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Science 18 November 1994:
Vol. 266. no. 5188, pp. 1241 - 1247
DOI: 10.1126/science.7526465
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Articles

Science, Vol 266, Issue 5188, 1241-1247
Copyright © 1994 by American Association for the Advancement of Science

articles

Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions

S Feng, JK Chen, H Yu, JA Simon, and SL Schreiber

Howard Hughes Medical Institute, Department of Chemistry, Harvard University, Cambridge, MA 02138.

Solution structures of two Src homology 3 (SH3) domain-ligand complexes have been determined by nuclear magnetic resonance. Each complex consists of the SH3 domain and a nine-residue proline-rich peptide selected from a large library of ligands prepared by combinatorial synthesis. The bound ligands adopt a left-handed polyproline type II (PPII) helix, although the amino to carboxyl directionalities of their helices are opposite. The peptide orientation is determined by a salt bridge formed by the terminal arginine residues of the ligands and the conserved aspartate-99 of the SH3 domain. Residues at positions 3, 4, 6, and 7 of both peptides also intercalate into the ligand-binding site; however, the respective proline and nonproline residues show exchanged binding positions in the two complexes. These structural results led to a model for the interactions of SH3 domains with proline-rich peptides that can be used to predict critical residues in complexes of unknown structure. The model was used to identify correctly both the binding orientation and the contact and noncontact residues of a peptide derived from the nucleotide exchange factor Sos in association with the amino-terminal SH3 domain of the adaptor protein Grb2.


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S. M. Ahern-Djamali, C. Bachmann, P. Hua, S. K. Reddy, A. S. Kastenmeier, U. Walter, and F. M. Hoffmann (1999)
PNAS 96, 4977-4982
   Abstract »    Full Text »    PDF »
Complexity in Chemistry.
G. M. Whitesides and R. F. Ismagilov (1999)
Science 284, 89-92
   Abstract »    Full Text »
Identification of a New Pyk2 Target Protein with Arf-GAP Activity.
J. Andreev, J.-P. Simon, D. D. Sabatini, J. Kam, G. Plowman, P. A. Randazzo, and J. Schlessinger (1999)
Mol. Cell. Biol. 19, 2338-2350
   Abstract »    Full Text »    PDF »
The Lck SH3 Domain Is Required for Activation of the Mitogen-activated Protein Kinase Pathway but Not the Initiation of T-cell Antigen Receptor Signaling.
M. F. Denny, H. C. Kaufman, A. C. Chan, and D. B. Straus (1999)
J. Biol. Chem. 274, 5146-5152
   Abstract »    Full Text »    PDF »
Multiple Isoforms of Heparan Sulfate D-Glucosaminyl 3-O-Sulfotransferase. ISOLATION, CHARACTERIZATION, AND EXPRESSION OF HUMAN cDNAs AND IDENTIFICATION OF DISTINCT GENOMIC LOCI.
N. W. Shworak, J. Liu, L. M. Petros, L. Zhang, M. Kobayashi, N. G. Copeland, N. A. Jenkins, and R. D. Rosenberg (1999)
J. Biol. Chem. 274, 5170-5184
   Abstract »    Full Text »    PDF »
SH3P7 Is a Cytoskeleton Adapter Protein and Is Coupled to Signal Transduction from Lymphocyte Antigen Receptors.
O. Larbolette, B. Wollscheid, J. Schweikert, P. J. Nielsen, and J. Wienands (1999)
Mol. Cell. Biol. 19, 1539-1546
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Cloning and Characterization of PRAX-1. A NEW PROTEIN THAT SPECIFICALLY INTERACTS WITH THE PERIPHERAL BENZODIAZEPINE RECEPTOR.
S. Galiegue, O. Jbilo, T. Combes, E. Bribes, P. Carayon, G. Le Fur, and P. Casellas (1999)
J. Biol. Chem. 274, 2938-2952
   Abstract »    Full Text »    PDF »
A contractile activity that closes phagosomes in macrophages.
J. Swanson, M. Johnson, K Beningo, P Post, M Mooseker, and N Araki (1999)
J. Cell Sci. 112, 307-316
   Abstract »    PDF »
A Sos-derived peptidimer blocks the Ras signaling pathway by binding both Grb2 SH3 domains and displays antiproliferative activity.
D. Cussac, M. Vidal, C. Leprince, W.-q. Liu, F. Cornille, G. Tiraboschi, B. P. Roques, and C. Garbay (1999)
FASEB J 13, 31-38
   Abstract »    Full Text »
Structural invariance of constitutively active and inactive mutants of Acanthamoeba myosin IC bound to F-actin in the rigor and ADP-bound states.
B. O. Carragher, N. Cheng, Z.-Y. Wang, E. D. Korn, A. Reilein, D. M. Belnap, J. A. Hammer III, and A. C. Steven (1998)
PNAS 95, 15206-15211
   Abstract »    Full Text »    PDF »
PSTPIP 2, a Second Tyrosine Phosphorylated, Cytoskeletal-associated Protein That Binds a PEST-type Protein-tyrosine Phosphatase.
Y. Wu, D. Dowbenko, and L. A. Lasky (1998)
J. Biol. Chem. 273, 30487-30496
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CdGAP, a Novel Proline-rich GTPase-activating Protein for Cdc42 and Rac.
N. Lamarche-Vane and A. Hall (1998)
J. Biol. Chem. 273, 29172-29177
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Structural Requirements for in Vivo Myosin I Function in Aspergillus nidulans.
N. Osherov, R. A. Yamashita, Y.-S. Chung, and G. S. May (1998)
J. Biol. Chem. 273, 27017-27025
   Abstract »    Full Text »    PDF »
Identification of a Novel Cortactin SH3 Domain-Binding Protein and Its Localization to Growth Cones of Cultured Neurons.
Y. Du, S. A. Weed, W.-C. Xiong, T. D. Marshall, and J. T. Parsons (1998)
Mol. Cell. Biol. 18, 5838-5851
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Grb2 Forms an Inducible Protein Complex with CD28 through a Src Homology 3 Domain-Proline Interaction.
K. Okkenhaug and R. Rottapel (1998)
J. Biol. Chem. 273, 21194-21202
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Association of p59fyn with the T Lymphocyte Costimulatory Receptor CD2. BINDING OF THE Fyn Src HOMOLOGY (SH) 3 DOMAIN IS REGULATED BY THE Fyn SH2 DOMAIN.
H. Lin, J. E. Hutchcroft, C. E. Andoniou, M. Kamoun, H. Band, and B. E. Bierer (1998)
J. Biol. Chem. 273, 19914-19921
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Growth Factor Receptor-Bound Protein 2 (Grb2) Association with Hemopoietic Specific Protein 1: Linkage Between Lck and Grb2.
Y. Takemoto, M. Furuta, M. Sato, P. R. Findell, W. Ramble, and Y. Hashimoto (1998)
J. Immunol. 161, 625-630
   Abstract »    Full Text »    PDF »
Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import.
M. Fransen, S. R. Terlecky, and S. Subramani (1998)
PNAS 95, 8087-8092
   Abstract »    Full Text »    PDF »
Role of the SH3-Ligand Domain of Simian Immunodeficiency Virus Nef in Interaction with Nef-Associated Kinase and Simian AIDS in Rhesus Macaques.
I. H. Khan, E. T. Sawai, E. Antonio, C. J. Weber, C. P. Mandell, P. Montbriand, and P. A. Luciw (1998)
J. Virol. 72, 5820-5830
   Abstract »    Full Text »    PDF »
Identification of a Candidate Human Spectrin Src Homology 3 Domain-binding Protein Suggests a General Mechanism of Association of Tyrosine Kinases with the Spectrin-based Membrane Skeleton.
D. Ziemnicka-Kotula, J. Xu, H. Gu, A. Potempska, K. S. Kim, E. C. Jenkins, E. Trenkner, and L. Kotula (1998)
J. Biol. Chem. 273, 13681-13692
   Abstract »    Full Text »    PDF »


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