2AL6

FERM domain of Focal Adhesion Kinase

2AL6 の概要

• エントリーDOI: 10.2210/pdb2al6/pdb
• 関連するPDBエントリー: 2AEH
• 分子名称: Focal adhesion kinase 1 (2 entities in total)
• 機能のキーワード: focal adhesion kinase ferm domain autophosphorylation site src sh3 binding site, transferase
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Cell junction, focal adhesion: Q00944
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 86029.65

構造登録者

Ceccarelli, D.F.,Song, H.K.,Poy, F.,Schaller, M.D.,Eck, M.J. (登録日: 2005-08-04, 公開日: 2005-10-18, 最終更新日: 2023-08-23)

主引用文献

Ceccarelli, D.F.,Song, H.K.,Poy, F.,Schaller, M.D.,Eck, M.J.
Crystal Structure of the FERM Domain of Focal Adhesion Kinase
J.Biol.Chem., 281:252-259, 2006

PubMed Abstract: Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that localizes to focal adhesions in adherent cells. Through phosphorylation of proteins assembled at the cytoplasmic tails of integrins, FAK promotes signaling events that modulate cellular growth, survival, and migration. The amino-terminal region of FAK contains a region of sequence homology with band 4.1 and ezrin/radixin/moesin (ERM) proteins termed a FERM domain. FERM domains are found in a variety of signaling and cytoskeletal proteins and are thought to mediate intermolecular interactions with partner proteins and phospholipids at the plasma membrane and intramolecular regulatory interactions. Here we report two crystal structures of an NH2-terminal fragment of avian FAK containing the FERM domain and a portion of the regulatory linker that connects the FERM and kinase domains. The tertiary folds of the three subdomains (F1, F2, and F3) are similar to those of known FERM structures despite low sequence conservation. Differences in the sequence and relative orientation of the F3 subdomain alters the nature of the interdomain interface, and the phosphoinositide binding site found in ERM family FERM domains is not present in FAK. A putative protein interaction site on the F3 lobe is masked by the proximal region of the linker. Additionally, in one structure the adjacent Src SH3 and SH2 binding sites in the linker associate with the surfaces of the F3 and F1 lobes, respectively. These structural features suggest the possibility that protein interactions of the FAK FERM domain can be regulated by binding of Src kinases to the linker segment.

PubMed: 16221668
DOI: 10.1074/jbc.M509188200

実験手法

X-RAY DIFFRACTION (2.35 Å)