1AOJ
THE SH3 DOMAIN OF EPS8 EXISTS AS A NOVEL INTERTWINED DIMER
Summary for 1AOJ
| Entry DOI | 10.2210/pdb1aoj/pdb |
| Descriptor | EPS8 (2 entities in total) |
| Functional Keywords | signal transduction, sh3 domain, eps8, proline rich peptide |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 14089.92 |
| Authors | Kishan, K.V.R.,Newcomer, M.E. (deposition date: 1997-07-07, release date: 1998-07-08, Last modification date: 2024-05-22) |
| Primary citation | Kishan, K.V.,Scita, G.,Wong, W.T.,Di Fiore, P.P.,Newcomer, M.E. The SH3 domain of Eps8 exists as a novel intertwined dimer. Nat.Struct.Biol., 4:739-743, 1997 Cited by PubMed Abstract: SH3 domains are structurally well-characterized as monomeric modular units of protein structure that mediate protein-protein recognition in numerous signal transduction proteins. The X-ray crystallographic structure of the Eps8 SH3 domain reveals a novel variation of the canonical SH3 fold: the SH3 domain from Eps8 is a dimer formed by strand interchange. In addition, co-immunoprecipitation experiments show that intact Eps8 is multimeric in vivo. Hence, the SH3 domain of Eps8 may represent a dimerization motif. PubMed: 9303002DOI: 10.1038/nsb0997-739 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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