Ontology highlight
ABSTRACT:
SUBMITTER: Wang X
PROVIDER: S-EPMC2475713 | biostudies-literature | 2008 Jul
REPOSITORIES: biostudies-literature
Wang Xiaoxia X Fukuda Koichi K Byeon In-Ja IJ Velyvis Algirdas A Wu Chuanyue C Gronenborn Angela A Qin Jun J
The Journal of biological chemistry 20080528 30
Alpha-parvin is an essential component of focal adhesions (FAs), which are large multiprotein complexes that link the plasma membrane and actin cytoskeleton. Alpha-parvin contains two calponin homology (CH) domains and its C-terminal CH2 domain binds multiple targets including paxillin LD motifs for regulating the FA network and signaling. Here we describe the solution structure of alpha-parvin CH2 bound to paxillin LD1. We show that although CH2 contains the canonical CH-fold, a previously defi ...[more]