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1AOJ

THE SH3 DOMAIN OF EPS8 EXISTS AS A NOVEL INTERTWINED DIMER

Summary for 1AOJ
Entry DOI10.2210/pdb1aoj/pdb
DescriptorEPS8 (2 entities in total)
Functional Keywordssignal transduction, sh3 domain, eps8, proline rich peptide
Biological sourceMus musculus (house mouse)
Total number of polymer chains2
Total formula weight14089.92
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 citationKishan, 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: 9303002
DOI: 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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