3T6G
Structure of the complex between NSP3 (SHEP1) and p130Cas
Summary for 3T6G
| Entry DOI | 10.2210/pdb3t6g/pdb |
| Related | 3T6A |
| Descriptor | SH2 domain-containing protein 3C, Breast cancer anti-estrogen resistance protein 1, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | cdc25-homology domain, gtpase exchange factor, focal-adhesion targeting domain, signaling protein, cell adhesion |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm (By similarity): Q8N5H7 Cell junction, focal adhesion: P56945 |
| Total number of polymer chains | 4 |
| Total formula weight | 125155.88 |
| Authors | Mace, P.D.,Robinson, H.,Riedl, S.J. (deposition date: 2011-07-28, release date: 2011-11-23, Last modification date: 2024-02-28) |
| Primary citation | Mace, P.D.,Wallez, Y.,Dobaczewska, M.K.,Lee, J.J.,Robinson, H.,Pasquale, E.B.,Riedl, S.J. NSP-Cas protein structures reveal a promiscuous interaction module in cell signaling. Nat.Struct.Mol.Biol., 18:1381-1387, 2011 Cited by PubMed Abstract: Members of the novel SH2-containing protein (NSP) and Crk-associated substrate (Cas) protein families form multidomain signaling platforms that mediate cell migration and invasion through a collection of distinct signaling motifs. Members of each family interact via their respective C-terminal domains, but the mechanism of this association has remained enigmatic. Here we present the crystal structures of the C-terminal domain from the NSP protein BCAR3 and the complex of NSP3 with p130Cas. BCAR3 adopts the Cdc25-homology fold of Ras GTPase exchange factors, but it has a 'closed' conformation incapable of enzymatic activity. The structure of the NSP3-p130Cas complex reveals that this closed conformation is instrumental for interaction of NSP proteins with a focal adhesion-targeting domain present in Cas proteins. This enzyme-to-adaptor conversion enables high-affinity, yet promiscuous, interactions between NSP and Cas proteins and represents an unprecedented mechanistic paradigm linking cellular signaling networks. PubMed: 22081014DOI: 10.1038/nsmb.2152 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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