2K2R

The NMR structure of alpha-parvin CH2/paxillin LD1 complex

Summary for 2K2R

• Entry DOI: 10.2210/pdb2k2r/pdb
• Descriptor: Alpha-parvin, Paxillin (2 entities in total)
• Functional Keywords: protein complex, actin-binding, alternative splicing, cell adhesion, cell junction, cytoplasm, cytoskeleton, lim domain, metal-binding, phosphoprotein, zinc
• Biological source: Homo sapiens (human)
• Cellular location: Cell junction, focal adhesion: Q9NVD7
• Total number of polymer chains: 2
• Total formula weight: 16098.43

Authors

Wang, X.,Fukuda, K.,Byeon, I.,Velyvis, A.,Wu, C.,Gronenborn, A.,Qin, J. (deposition date: 2008-04-10, release date: 2008-05-27, Last modification date: 2024-05-29)

Primary citation

Wang, X.,Fukuda, K.,Byeon, I.J.,Velyvis, A.,Wu, C.,Gronenborn, A.,Qin, J.
The Structure of {alpha}-Parvin CH2-Paxillin LD1 Complex Reveals a Novel Modular Recognition for Focal Adhesion Assembly.
J.Biol.Chem., 283:21113-21119, 2008

PubMed Abstract: 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 defined N-terminal linker forms an alpha-helix that packs unexpectedly with the C-terminal helix of CH2, resulting in a novel variant of the CH domain. Importantly, such packing generates a hydrophobic surface that recognizes the Leu-rich face of paxillin-LD1, and the binding pattern differs drastically from the classical paxillin-LD binding to four-helix bundle proteins such as focal adhesion kinase. These results define a novel modular recognition mode and reveal how alpha-parvin associates with paxillin to mediate the FA assembly and signaling.

PubMed: 18508764
DOI: 10.1074/jbc.M801270200

Experimental method

SOLUTION NMR