1qvx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qvx.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1qvx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qvx| PDB=1qvx | SCENE= }}
{{STRUCTURE_1qvx| PDB=1qvx | SCENE= }}
-
'''SOLUTION STRUCTURE OF THE FAT DOMAIN OF FOCAL ADHESION KINASE'''
+
===SOLUTION STRUCTURE OF THE FAT DOMAIN OF FOCAL ADHESION KINASE===
-
==Overview==
+
<!--
-
Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that is regulated by integrins. Upon activation, FAK generates signals that modulate crucial cell functions, including cell proliferation, migration, and survival. The C-terminal focal adhesion targeting (FAT) sequence mediates localization of FAK to discrete regions in the cell called focal adhesions. Several binding partners for the FAT domain of FAK have been identified, including paxillin. We have determined the solution structure of the avian FAT domain in complex with a peptide mimicking the LD2 motif of paxillin by NMR spectroscopy. The FAT domain retains a similar fold to that found in the unliganded form when complexed to the paxillin-derived LD2 peptide, an antiparallel four-helix bundle. However, noticeable conformational changes were observed upon the LD2 peptide binding, especially the position of helix 4. Multiple lines of evidence, including the results obtained from isothermal titration calorimetry, intermolecular nuclear Overhauser effects, mutagenesis, and protection from paramagnetic line broadening, support the existence of two distinct paxillin-binding sites on the opposite faces of the FAT domain. The structure of the FAT domain-LD2 complex was modeled using the program HADDOCK based on our solution structure of the LD2-bound FAT domain and mutagenesis data. Our model of the FAT domain-LD2 complex provides insight into the molecular basis of FAK-paxillin binding interactions, which will aid in understanding the role of paxillin in FAK targeting and signaling.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14662767}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14662767 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14662767}}
==About this Structure==
==About this Structure==
-
1QVX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVX OCA].
+
1QVX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVX OCA].
==Reference==
==Reference==
Line 36: Line 40:
[[Category: Helix bundle]]
[[Category: Helix bundle]]
[[Category: Nmr]]
[[Category: Nmr]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:45:41 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:26:27 2008''

Revision as of 07:26, 28 July 2008

Image:1qvx.png

Template:STRUCTURE 1qvx

SOLUTION STRUCTURE OF THE FAT DOMAIN OF FOCAL ADHESION KINASE

Template:ABSTRACT PUBMED 14662767

About this Structure

1QVX is a Single protein structure of sequence from Gallus gallus. Full experimental information is available from OCA.

Reference

NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model., Gao G, Prutzman KC, King ML, Scheswohl DM, DeRose EF, London RE, Schaller MD, Campbell SL, J Biol Chem. 2004 Feb 27;279(9):8441-51. Epub 2003 Dec 7. PMID:14662767

Page seeded by OCA on Mon Jul 28 10:26:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qvx"
Personal tools