2jx0
From Proteopedia
The paxillin-binding domain (PBD) of G Protein Coupled Receptor (GPCR)-kinase (GRK) interacting protein 1 (GIT1)
Overview
The G Protein Coupled Receptor (GPCR)-kinase (GRK) interacting protein 1 (GIT1) is a multidomain protein that plays an important role in cell adhesion, motility, cytoskeletal remodeling, and membrane trafficking. GIT1 mediates the localization of p21-activated kinase (PAK) and PAK-interactive exchange factor (PIX) to focal adhesions, and its activation is regulated by the interaction between its C-terminal paxillin-binding domain (PBD) and the LD motifs of paxillin. In this study, we determined the solution structure of rat GIT1 PBD by nuclear magnetic resonance (NMR) spectroscopy. The PBD folds into a four-helix bundle, which is structurally similar to the focal adhesion targeting (FAT) domain and the vinculin tail (Vt) domain. Previous studies showed that GIT1 interacts with paxillin through the LD4 motif. Here, we demonstrated that in addition to the LD4 motif, the GIT1 PBD can also bind to the paxillin LD2 motif; and both LD2 and LD4 motifs competitively target the same site on the PBD surface. We also revealed that paxillin S272 phosphorylation does not influence GIT1 PBD binding in vitro. These results are in agreement with the notion that phosphorylation of paxillin S272 plays an essential role in regulating focal adhesion turnover.
About this Structure
2JX0 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
GIT1 paxillin-binding domain is a four-helix bundle and it binds to both paxillin LD2 and LD4 motifs., Zhang ZM, Simmerman JA, Guibao CD, Zheng JJ, J Biol Chem. 2008 Apr 30;. PMID:18448431 Page seeded by OCA on Thu May 22 22:25:27 2008
