2QMS
Crystal structure of a signaling molecule
Summary for 2QMS
| Entry DOI | 10.2210/pdb2qms/pdb |
| Descriptor | Growth factor receptor-bound protein 7, SULFATE ION (3 entities in total) |
| Functional Keywords | sh2 domain, alpha/beta fold, signaling protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 55435.28 |
| Authors | Porter, C.J.,Wilce, M.C.,Wilce, J.A. (deposition date: 2007-07-16, release date: 2008-07-22, Last modification date: 2024-02-21) |
| Primary citation | Porter, C.J.,Matthews, J.M.,Mackay, J.P.,Pursglove, S.E.,Schmidberger, J.W.,Leedman, P.J.,Pero, S.C.,Krag, D.N.,Wilce, M.C.,Wilce, J.A. Grb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferation. Bmc Struct.Biol., 7:58-58, 2007 Cited by PubMed Abstract: Human growth factor receptor bound protein 7 (Grb7) is an adapter protein that mediates the coupling of tyrosine kinases with their downstream signaling pathways. Grb7 is frequently overexpressed in invasive and metastatic human cancers and is implicated in cancer progression via its interaction with the ErbB2 receptor and focal adhesion kinase (FAK) that play critical roles in cell proliferation and migration. It is thus a prime target for the development of novel anti-cancer therapies. Recently, an inhibitory peptide (G7-18NATE) has been developed which binds specifically to the Grb7 SH2 domain and is able to attenuate cancer cell proliferation and migration in various cancer cell lines. PubMed: 17894853DOI: 10.1186/1472-6807-7-58 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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