This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ktm
From Proteopedia
Revision as of 17:56, 28 September 2014 by OCA (Talk | contribs)
1ktm is a 1 chain structure with sequence from Gallus gallus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Focal adhesion kinase (FAK) is a nonreceptor tyrosine kinase whose focal adhesion targeting (FAT) domain interacts with other focal adhesion molecules in integrin-mediated signaling. Localization of activated FAK to focal adhesions is indispensable for its function. Here we describe a solution structure of the FAT domain bound to a peptide derived from paxillin, a FAK-binding partner. The FAT domain is composed of four helices that form a "right-turn" elongated bundle; the globular fold is mainly maintained by hydrophobic interactions. The bound peptide further stabilizes the structure. Certain signaling events such as phosphorylation and molecule interplay may induce opening of the helix bundle. Such conformational change is proposed to precede departure of FAK from focal adhesions, which starts focal adhesion turnover.
Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase.,Liu G, Guibao CD, Zheng J Mol Cell Biol. 2002 Apr;22(8):2751-60. PMID:11909967[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Liu G, Guibao CD, Zheng J. Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase. Mol Cell Biol. 2002 Apr;22(8):2751-60. PMID:11909967
