TY  - JOUR
N1  - Copyright of this article belongs to NPG.
ID  - open771
UR  - http://crdd.osdd.net/open/771/
IS  - 9
A1  - Kishan, K V Radha
A1  - Scita, G
A1  - Wong, W T
A1  - Di Fiore, P P
A1  - Newcomer, M E
Y1  - 1997/09//
N2  - 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.
PB  - NPG
JF  - Nature structural biology
VL  - 4
SN  - 1072-8368
TI  - The SH3 domain of Eps8 exists as a novel intertwined dimer.
SP  - 739
AV  - none
EP  - 43
ER  -