1ktm
From Proteopedia
(New page: 200px<br /><applet load="1ktm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ktm" /> '''SOLUTION STRUCTURE OF FAT DOMAIN OF FOCAL AD...) |
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'''SOLUTION STRUCTURE OF FAT DOMAIN OF FOCAL ADHESION KINASE'''<br /> | '''SOLUTION STRUCTURE OF FAT DOMAIN OF FOCAL ADHESION KINASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Focal adhesion kinase (FAK) is a nonreceptor tyrosine kinase whose focal | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1KTM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http:// | + | 1KTM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: nmr]] | [[Category: nmr]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:48 2008'' |
Revision as of 11:37, 21 February 2008
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SOLUTION STRUCTURE OF FAT DOMAIN OF FOCAL ADHESION KINASE
Overview
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.
About this Structure
1KTM is a Single protein structure of sequence from Gallus gallus. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
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
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