1kl0: Difference between revisions
No edit summary |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
{{Theoretical_model}} | {{Theoretical_model}} | ||
[[ | ==THEORETICAL MODEL OF THE FAT DOMAIN OF FOCAL ADHESION KINASE COMPLEXED WITH PAXILLIN LD2 MOTIF== | ||
<StructureSection load='1kl0' size='340' side='right'caption='[[1kl0]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KL0 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kl0 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1kl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kl0 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Focal adhesion kinase (FAK) is a tyrosine kinase found in focal adhesions, intracellular signaling complexes that are formed following engagement of the extracellular matrix by integrins. The C-terminal 'focal adhesion targeting' (FAT) region is necessary and sufficient for localizing FAK to focal adhesions. We have determined the crystal structure of FAT and show that it forms a four-helix bundle that resembles those found in two other proteins involved in cell adhesion, alpha-catenin and vinculin. The binding of FAT to the focal adhesion protein, paxillin, requires the integrity of the helical bundle, whereas binding to another focal adhesion protein, talin, does not. We show by mutagenesis that paxillin binding involves two hydrophobic patches on opposite faces of the bundle and propose a model in which two LD motifs of paxillin adopt amphipathic helices that augment the hydrophobic core of FAT, creating a six-helix bundle. | |||
The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin.,Hayashi I, Vuori K, Liddington RC Nat Struct Biol. 2002 Feb;9(2):101-6. PMID:11799401<ref>PMID:11799401</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1kl0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Hayashi, I]] | [[Category: Hayashi, I]] | ||
[[Category: Liddington, R C]] | [[Category: Liddington, R C]] | ||
[[Category: Vuori, K]] | [[Category: Vuori, K]] | ||
Latest revision as of 09:54, 11 August 2021
 |
THEORETICAL MODEL OF THE FAT DOMAIN OF FOCAL ADHESION KINASE COMPLEXED WITH PAXILLIN LD2 MOTIFTHEORETICAL MODEL OF THE FAT DOMAIN OF FOCAL ADHESION KINASE COMPLEXED WITH PAXILLIN LD2 MOTIF
Structural highlights
Publication Abstract from PubMedFocal adhesion kinase (FAK) is a tyrosine kinase found in focal adhesions, intracellular signaling complexes that are formed following engagement of the extracellular matrix by integrins. The C-terminal 'focal adhesion targeting' (FAT) region is necessary and sufficient for localizing FAK to focal adhesions. We have determined the crystal structure of FAT and show that it forms a four-helix bundle that resembles those found in two other proteins involved in cell adhesion, alpha-catenin and vinculin. The binding of FAT to the focal adhesion protein, paxillin, requires the integrity of the helical bundle, whereas binding to another focal adhesion protein, talin, does not. We show by mutagenesis that paxillin binding involves two hydrophobic patches on opposite faces of the bundle and propose a model in which two LD motifs of paxillin adopt amphipathic helices that augment the hydrophobic core of FAT, creating a six-helix bundle. The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin.,Hayashi I, Vuori K, Liddington RC Nat Struct Biol. 2002 Feb;9(2):101-6. PMID:11799401[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||