1k40: Difference between revisions

Revision as of 14:29, 21 February 2008

crystal structure of the FAT domain of focal adhesion kinase

OverviewOverview

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.

About this StructureAbout this Structure

1K40 is a Single protein structure of sequence from Mus musculus. 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.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 13:29:54 2008

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OCA

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-[[Image:1k40.gif|left|200px]]<br /><applet load="1k40" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1k40.gif|left|200px]]<br /><applet load="1k40" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1k40, resolution 2.25&Aring;" />
 '''crystal structure of the FAT domain of focal adhesion kinase'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-K40 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K40 OCA].
+K40 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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=1K40 OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Transferase]]
 [[Category: Hayashi, I.]]
-[[Category: Liddington, R.C.]]
+[[Category: Liddington, R C.]]
 [[Category: Vuori, K.]]
 [[Category: helix bundle]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:50:29 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:54 2008''