1MW4
Solution structure of the human Grb7-SH2 domain in complex with a 10 amino acid peptide pY1139
Summary for 1MW4
| Entry DOI | 10.2210/pdb1mw4/pdb |
| Descriptor | Growth factor receptor-bound protein 7, Receptor protein-tyrosine kinase erbB-2 (2 entities in total) |
| Functional Keywords | sh2 domain in complex with a ligand, hormone-growth factor-transferase complex, hormone/growth factor/transferase |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm: Q14451 Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cytoplasm. Isoform 3: Cytoplasm: P04626 |
| Total number of polymer chains | 2 |
| Total formula weight | 14956.92 |
| Authors | Ivancic, M.,Lyons, B.A. (deposition date: 2002-09-27, release date: 2003-09-09, Last modification date: 2024-10-16) |
| Primary citation | Ivancic, M.,Daly, R.J.,Lyons, B.A. Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2 J.BIOMOL.NMR, 27:205-219, 2003 Cited by PubMed Abstract: The solution structure of the hGrb7-SH2 domain in complex with a ten amino acid phosphorylated peptide ligand representative of the erbB2 receptor tyrosine kinase (pY1139) is presented as determined by nuclear magnetic resonance methods. The hGrb7-SH2 domain structure reveals the Src homology 2 domain topology consisting of a central beta-sheet capped at each end by an alpha-helix. The presence of a four residue insertion in the region between beta-strand E and the EF loop and resulting influences on the SH2 domain/peptide complex structure are discussed. The binding conformation of the erbB2 peptide is in a beta-turn similar to that found in phosphorylated tyrosine peptides bound to the Grb2-SH2 domain. To our knowledge this is only the second example of an SH2 domain binding its naturally occurring ligands in a turn, instead of extended, conformation. Close contacts between residues responsible for binding specificity in hGrb7-SH2 and the erbB2 peptide are characterized and the potential effect of mutation of these residues on the hGrb7-SH2 domain structure is discussed. PubMed: 12975581DOI: 10.1023/A:1025498409113 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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