Abstract
Non-covalent molecular interactions in biological systems are ubiquitous and finely tuned. While enzyme substrate complexes are relatively well understood and considerable knowledge has been gained recently about the way proteins interact with DNA (Harrison, 1991), understanding of protein-protein interactions is relatively poor. Many complexes involving proteins are large and apparently intractable for structural studies. Examples of interest include: cell-cell interactions mediated by different adhesion molecules; a cytokine bound to a membrane receptor; a tyrosine kinase bound to a protein substrate; a blood clotting complex. In cases where there is information available about protein-protein interactions, e.g. in antibody/protein antigen complexes, the interacting protein surface patches seem to involve more than one peptide loop from different parts of the protein sequence (Chothia, 1991).
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Atkinson, A. and Williams, R. J. P. (1990). Solution structure of the kringle 4 domain from human plasminogen by 1H NMR and distance geometry. J. Mol. Biol., 212, 541–552
Barlow, P. N., Norman, D. G., Steinkasserer, A., Horne, T. J., Pearce, J. M., Driscoll, P. C., Sim, R. B. and Campbell, I. D. (1992). Solution structure of the fifth repeat of factor H—a second example of the complement control protein module. Biochemistry, 31, 3626–3634
Baron, M., Main, A. L., Driscoll, P. C., Mardon, H. J., Boyd, J. and Campbell I. D. (1992a). 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin. Biochemistry, 31, 2068–2073
Baron M., Norman, D. G. and Campbell, I. D. (1991). Protein modules. TIBS, 16, 13–17
Baron, M. Norman, D. G., Harvey, T. S., Handford, P. A., Mayhew, M., Tse, A. G. D., Brownlee, G. G. and Campbell, I. D. (1992b). The 3D structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-α. Protein Sci., 1, 81–90
Baron, M. Norman, D. G., Willis, A. and Campbell, I. D. (1990). Structure of the fibronectin type 1 module. Nature, 345, 642–646
Bax, A. Experimental techniques for studies of biopolymers. Curr. Topics Struct. Biol., 1, 1030–1035
Bennett, W. A. F., Paoni, N. F., Keyt, B. A., Bolstein, D., Jones, A. J. S., Presta, L., Wurm, F. M. and Zoller, M. J. (1991). High resolution analysis of functional determinants on human tPA. J. Biol. Chem., 266, 5191–5201
Brown, S. C., Weber, P. L. and Mueller, L. (1987). Toward complete 1H NMR spectra in proteins. J. Magn. Reson., 77, 166–169
Brünger, A. T. (1988). XPLOR Manual. Yale University, New Haven, CT
Brünger, A. T., Clore, G. M., Gronenborn, A. M. and Karplus, M. (1987). Solution conformations of human growth hormone releasing factor: comparison of the restrained molecular dynamics and distance geometry methods for a system without long-range distance data. Protein Engng, 1, 399–406
Byeon, I. L. and Llinas, M. (1991). Solution structure of the tissue type plasminogen activator kringle 2 domain complexed to 6-aminohexanoic acid, an antifibrinolytic drug. J. Mol. Biol., 222, 1035–1051
Campbell, I. D. and Baron, M. (1991). The structure and function of protein modules. Phil. Trans. Roy. Soc. Lond., B332, 165–170
Chothia, C. (1991). Antigen recognition Curr. Opinion Struct. Biol., 1, 53–59
Clayton, L. K., Sayre, P. H., Novotny, J. and Reinherz, E. L. (1987). Murine and human T11 (CD2) cDNA sequences suggest a common signal transduction mechanism. Eur. J. Immunol., 17, 1367–1370
Clore, G. M., Brünger, A. T., Karplus, M. and Gronenborn, A. M. (1986). Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination: a model study of crambin. J. Mol. Biol., 191, 523–551
Clore, G. M. and Gronenborn A. M. (1991a). Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy. Science, 252, 1390–1399
Clore, G. M. and Gronenborn, A. M. (1991b). Two-, three-, and four-dimensional NMR methods for obtaining larger and more precise three-dimensional structures of proteins in solution. Ann. Rev. Biophys. Biophys. Chem. 20, 29–63
Constantine, K. L., Ramesh, V., Banyai, L., Trexler, M., Patthy, L. and Llinas, M. (1991). Sequence-specific 1H NMR assignments and structural characterisation of bovine seminal fluid protein PDC-109 domain b. Biochemistry, 30, 1663–1672
Cooke, R. M., Wilkinson, A. J., Baron, M., Pastore, A., Tappin, M. J., Campbell, I. D., Gregory, H. and Sheard, B. (1987). The solution structure of human epidermal growth factor. Nature, 327, 339–341
Doolittle, R. F. (1989). Similar amino-acids revisited. TIBS, 14, 244–245
Dorit, R. L. and Gilbert, W. A. (1991). The limited universe of exons. Curr. Opinion Struct. Biol., 1, 973–977
Downing, A. K., Driscoll, P. C., Harvey, T. S., Dudgeon, T. J., Smith, B. O., Baron, M. and Campbell, I. D. (1993). The solution structure of the fibrin binding finger domain of tissue-type plasminogen activator determined by 1H NMR. J. Mol. Biol. (in press)
Driscoll, P. C., Clore, G. M., Beress, L. and Gronenborn, A. M. (1989). A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: Sequential and stereospecific resonance assignment and secondary structure. Biochemistry, 28, 2178–2187
Driscoll, P. C., Cyster, J., Campbell, I. D. and Williams, A. F. (1991). Structure of domain 1 of rat T lymphocyte CD2 antigen. Nature, 353, 762–765
Dustin, M. L. and Springer, T. A. (1991). Role of lymphocyte adhesion receptors in transient interactions and cell locomotion. Ann. Rev. Immunol., 9, 27–66
Engel, J. (1991). Common structural motifs in proteins of the extracellular matrix. Curr. Opinion Cell Biol., 3, 779–785
Furie, B. and Furie, B. C. (1988). The molecular basis of blood coagulation. Cell, 53, 505–517
Haber, E., Quertermous T., Matsueda, G. R. and Runge, M. S. (1989). Innovative approaches to plasminogen activator therapy. Science, 243, 51–56
Handford, P. A., Baron, M., Mayhew, M., Willis, A., Beesley, T., Brownlee, G. G. and Campbell, I. D. (1990). The first EGF-like domain of human factor IX has a high affinity Ca++ binding site. EMBO Jl, 9, 475–480
Handford, P. A., Mayhew, M., Baron, M., Winship, P. R., Campbell, I. D. and Brownlee, G. G. (1991). Key residues involved in calcium-binding motifs in EGF-like domains. Nature, 351, 164–167
Harrison, S. C. (1991). The structural taxonomy of DNA-binding domains. Nature, 353, 715–719
Holmgren, A., Kuehn, M. J., Bränden, C.-I. and Hultgren, S. J. (1992). Conserved immuno-globulin-like features in a family of periplasmic pilus chaperones in bacteria. EMBO Jl, 16, 1617–1622
Hommel, U., Dudgeon, T. J., Fallon, A., Edwards, R. M. and Campbell, I. D. (1991). Structure-function relationship in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR. Biochemistry, 30, 8891–8
Hommel, U., Harvey, T. S., Driscoll, P. C. and Campbell, I. D. (1992). Human epidermal growth factor: high resolution solution structure and comparison with human TGF-α. J. Mol. Biol. (in press)
Kay L. E. and Bax A. (1990). New methods for the measurement of NH-CαH coupling constants in 15N-labeled proteins. J. Magn. Reson., 86, 110–126
Kay, L. E., Torchia, D. A. and Bax, A. (1989). Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR: application to staphylococcal nuclease. Biochemistry, 28, 8972–8979
Kraulis, P. J. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog., 24, 946–950
Mallett, S., Fossum, S. and Barclay, A. N. (1990). Characterization of the MRC OX40 antigen of activated CD4 positive T lymphocytes—a molecule related to nerve growth factor receptor. EMBO Jl, 9, 1063–1068
Marion, D. and Bax, A. (1988). Baseline distortion in real-Fourier-transform NMR spectra. J. Magn. Reson., 79, 352–356
Marion, D., Ikura, M. and Bax, A. (1989). Improved solvent suppression in one- and two-dimensional NMR spectra by convolution of time-domain data. J. Magn. Reson., 84, 425–430
Messerle, B. A., Wider, G., Otting, G., Weber, G. and Wüthrich, K. (1989). Solvent suppression using a spin lock in 2D and 3D NMR spectroscopy with H2O solutions. J. Magn. Reson., 85, 608–613
Montelione, G. T., Wüthrich, K., Nice, E. C., Burgess, A. W. and Sheraga, H. A. (1987). Solution structure of murine EGF; determination of the polypeptide backbone chain-fold by NMR and distance geometry. Proc. Natl Acad. Sci. USA, 84, 5226–5230
Müller, L. (1987). P. E. COSY, a simple alternative to E. COSY. J. Magn. Reson., 72, 191–196
Nilges, M., Clore, G. M. and Gronenborn, A. M. (1990). 1H-NMR stereospecific assignments by conformational data-base searches. Biopolymers, 29, 813–822
Nilges, M., Gronenborn, A. M., Brünger, A. T. and Clore, G. M. (1988). Determination of three-dimensional structure of proteins by simulated annealing with interproton distance restraints: Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. Protein Engng, 2, 27–38
Norman, D. G., Barlow, P. N., Baron, M., Day, A. J., Sim, R. B. and Campbell, I. D. (1991). Three-dimensional structure of a complement control protein module in solution. J. Mol. Biol., 219, 717–725
Norwood, T. J., Crawford, D. A., Stevenson, M. E., Driscoll, P. C. and Campbell, I. D. (1993). 1H-15N nuclear magnetic resonance studies of the c subunit of the E. coli F1F0 ATP synthase: assignment and secondary structure. Biochemistry (in press)
Novokhatny, V. V., Ingham, K. C. and Medved, L. V. (1991). Domain structure and domain-domain interactions of recombinant tPA. J. Biol. Chem., 266, 12994–13002
Patthy L. (1985). Evolution of the proteases of the blood clotting and fibrinolysis by assembly from modules. Cell, 41, 657–663
Patthy, L. (1987). Intron-dependent evolution: preferred types of exons and introns. FEBS Lett., 214, 1–7
Patthy, L. (1991). Modular exchange principles in proteins. Curr. Opinion Struct. Biol., 1, 351–361
Peterson, A. and Seed B. (1987). Monoclonal antibody and ligand binding sites of the T-cell erythrocyte receptor (CD2). Nature, 329, 842–846
Plateau, P. and Guéron, M. (1982). Exchangeable proton NMR without base-line distortion, using new strong-pulse sequences. J. Am. Chem. Soc., 104, 7310–7311
Recny, M. A., Neidhart, E. A., Sayre, P. H., Ciardelli, T. L. and Reinherz, E. L. (1990). Structural and functional characterisation of the CD2 immuno-adhesive domain. J. Biol. Chem., 265, 8542–8549
Redfield, C. and Dobson, C. M. (1990). 1H NMR studies of human lysozyme: Spectral assignment and comparison with hen lysozyme. Biochemistry, 29, 7201–7214
Reid, K. B. M. and Day, A. J. (1989). Structure function relationships of the complement system. Immunol. Today, 10, 177–180
Ryu, S. E., Kwong, P. D., Truneh, A., Porter, T. G., Arthos, J., Rosenberg, M., Dai, X., Xuong, N., Axel, R., Sweet, R. W. and Hendrickson, W. A. (1990). Crystal structure of HIV-binding recombinant fragment of human CD4. Nature, 348, 419–426
Selander, M., Persson, E., Stenflo, J. and Drakenberg, T. (1990). 1H assignment and secondary structure of the Ca2+ form of the amino-terminal epidermal growth factor like domain in coagulation factor X. Biochemistry, 29, 8111–8
Soriano-Garcia, M., Padmanabhan, K., de Vos, A. M. and Tulinsky, A. (1992). The Ca++ ion and membrane binding structure of the gla domain of Ca-prothrombin fragment 1. Biochemistry, 31, 2554–2566
Soriano-Garcia, M., Park, C. H., Tulinsky, A., Ravichandran, K. G. and Skrzpzcak-Jankun, E. (1989). Structure of Ca++ prothrombin fragment 1 including the conformation of the gla domain. Biochemistry, 28, 6805–6810
Soutar, A. K. and Knight, B. L. (1990). Structure and regulation of the LDL-receptor and its gene. Br. Med. Bull., 46, 891–916
Springer, T. A. (1990). Adhesion receptors of the immune system. Nature, 346, 425–434
Spruyt, L. L., Glennie, M. J., Beyers, A. D. and Williams, A. F. (1991). Signal transduction by the CD2 antigen T cells and natural killer cells: Requirement for expression of a functional T cell receptor or binding of antibody Fc to the receptor, FcγRIIIA (CD16). J. Exptl Med., 174, 1407–1415
Tappin, M. J. Cooke, R. M., Fitton, J. E. and Campbell, I. D. (1989). A high resolution 1H NMR study of human transforming growth factor α: structure and pH dependent conformational interconversion. Eur. J. Biochem., 179, 629–637
de Vos, A. M., Ultsch, M. H., Kelley, R. F., Padmanabhan, K., Tulinsky, A., Westbrook, M. L. and Kossiakof, A. A. (1992a). Crystal structure of the kringle 2 domain of tissue plasminogen activator at 2.4Å resolution. Biochemistry, 31, 270–279
de Vos, A. M., Ultsch, M. and Kossiakof, A. A. (1992b). Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science, 255, 306–312
Wang, J., Yan, Y., Garret, T. P. J., Liu, J., Rodgers, D. W., Garlick, R. L., Tarr, G. E., Hussain, Y., Reinherz, E. L. and Harrison, S. C. (1990). Atomic structure of a fragment of CD4 containing two immunoglobulin-like domains. Nature, 348, 411–419
Weis, W. I., Kahn, R., Fourme, R., Drickamer, K. and Hendrickson, W. A. (1991). Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing. Science, 254, 1608–1615
Williams, A. F. (1987). A year in the life of the immunoglobulin superfamily. Immunol. Today, 8, 298–303
Williams, A. F. and Barclay, A. N. (1988). The immunoglobulin superfamily—domains for cell surface recognition. Ann. Rev. Immunol., 6, 381–405
Witwer, A. J. and Howard, S. C. (1990). Glycosylation at Asn-184 inhibits the conversion of single chain to two-chain tPA by plasmin. Biochemistry, 29, 4175–4180
Wüthrich, K. (1986). NMR of Proteins and Nucleic Acids. New York, Wiley
Wüthrich, K. (1989). Protein structure determination in solution by NMR. Science, 243, 45–50
Yamada, K. M. (1991). Adhesive recognition sequences. J. Biol. Chem., 266, 12809–12812
Editor information
Editors and Affiliations
Copyright information
© 1993 The contributors
About this chapter
Cite this chapter
Campbell, I.D., Driscoll, P.C. (1993). NMR Studies of the Structure and Role of Modules Involved in Protein-Protein Interactions. In: Clore, G.M., Gronenborn, A.M. (eds) NMR of Proteins. Topics in Molecular and Structural Biology. Palgrave, London. https://doi.org/10.1007/978-1-349-12749-8_5
Download citation
DOI: https://doi.org/10.1007/978-1-349-12749-8_5
Publisher Name: Palgrave, London
Print ISBN: 978-1-349-12751-1
Online ISBN: 978-1-349-12749-8
eBook Packages: EngineeringEngineering (R0)