1pv3

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[[Image:1pv3.jpg|left|200px]]<br /><applet load="1pv3" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pv3.jpg|left|200px]]
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caption="1pv3" />
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'''NMR Solution Structure of the Avian FAT-domain of Focal Adhesion Kinase'''<br />
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{{Structure
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|PDB= 1pv3 |SIZE=350|CAPTION= <scene name='initialview01'>1pv3</scene>
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|SITE=
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|LIGAND=
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|ACTIVITY= [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]
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|GENE= FAK1 OR FAK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])
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}}
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'''NMR Solution Structure of the Avian FAT-domain of Focal Adhesion Kinase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1PV3 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=1PV3 OCA].
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1PV3 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=1PV3 OCA].
==Reference==
==Reference==
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The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation., Prutzman KC, Gao G, King ML, Iyer VV, Mueller GA, Schaller MD, Campbell SL, Structure. 2004 May;12(5):881-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15130480 15130480]
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The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation., Prutzman KC, Gao G, King ML, Iyer VV, Mueller GA, Schaller MD, Campbell SL, Structure. 2004 May;12(5):881-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15130480 15130480]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: helix bundle]]
[[Category: helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:29:23 2008''

Revision as of 11:29, 20 March 2008


PDB ID 1pv3

Drag the structure with the mouse to rotate
Gene: FAK1 OR FAK (Gallus gallus)
Activity: Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2
Coordinates: save as pdb, mmCIF, xml



NMR Solution Structure of the Avian FAT-domain of Focal Adhesion Kinase


Overview

The focal adhesion targeting (FAT) domain of focal adhesion kinase (FAK) is critical for recruitment of FAK to focal adhesions and contains tyrosine 926, which, when phosphorylated, binds the SH2 domain of Grb2. Structural studies have shown that the FAT domain is a four-helix bundle that exists as a monomer and a dimer due to domain swapping of helix 1. Here, we report the NMR solution structure of the avian FAT domain, which is similar in overall structure to the X-ray crystal structures of monomeric forms of the FAT domain, except that loop 1 is longer and less structured in solution. Residues in this region undergo temperature-dependent exchange broadening and sample aberrant phi and psi angles, which suggests that this region samples multiple conformations. We have also identified a mutant that dimerizes approximately 8 fold more than WT FAT domain and exhibits increased phosphorylation of tyrosine 926 both in vitro and in vivo.

About this Structure

1PV3 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation., Prutzman KC, Gao G, King ML, Iyer VV, Mueller GA, Schaller MD, Campbell SL, Structure. 2004 May;12(5):881-91. PMID:15130480

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