1aoj | pdb_00001aoj
From Proteopedia
THE SH3 DOMAIN OF EPS8 EXISTS AS A NOVEL INTERTWINED DIMER
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSH3 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. The SH3 domain of Eps8 exists as a novel intertwined dimer.,Kishan KV, Scita G, Wong WT, Di Fiore PP, Newcomer ME Nat Struct Biol. 1997 Sep;4(9):739-43. PMID:9303002[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. ReferencesContents | ||||||||||||||||
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