1qvx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:03, 9 May 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1qvx.png|left|200px]]
 
-
<!--
+
==SOLUTION STRUCTURE OF THE FAT DOMAIN OF FOCAL ADHESION KINASE==
-
The line below this paragraph, containing "STRUCTURE_1qvx", creates the "Structure Box" on the page.
+
<StructureSection load='1qvx' size='340' side='right'caption='[[1qvx]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1qvx]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QVX FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1qvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qvx OCA], [https://pdbe.org/1qvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qvx RCSB], [https://www.ebi.ac.uk/pdbsum/1qvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qvx ProSAT]</span></td></tr>
-
{{STRUCTURE_1qvx| PDB=1qvx | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FAK1_CHICK FAK1_CHICK] Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development, embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), ephrin receptors, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Regulates P53/TP53 activity and stability. Phosphorylates SRC; this increases SRC kinase activity. Isoform 2 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling.<ref>PMID:15494733</ref> <ref>PMID:15494734</ref> <ref>PMID:15494732</ref> <ref>PMID:20705914</ref> <ref>PMID:21852560</ref> <ref>PMID:21937583</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qv/1qvx_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qvx ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
===SOLUTION STRUCTURE OF THE FAT DOMAIN OF FOCAL ADHESION KINASE===
+
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<ref>PMID:14662767</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1qvx" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_14662767}}, adds the Publication Abstract to the page
+
*[[Focal adhesion kinase 3D structures|Focal adhesion kinase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 14662767 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_14662767}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1QVX is a 1 chain 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==
+
-
<ref group="xtra">PMID:14662767</ref><references group="xtra"/>
+
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
-
[[Category: Transferase]]
+
[[Category: Large Structures]]
-
[[Category: Campbell, S L.]]
+
[[Category: Campbell SL]]
-
[[Category: DeRose, E F.]]
+
[[Category: DeRose EF]]
-
[[Category: Gao, G.]]
+
[[Category: Gao G]]
-
[[Category: King, M L.]]
+
[[Category: King ML]]
-
[[Category: London, R E.]]
+
[[Category: London RE]]
-
[[Category: Prutzman, K C.]]
+
[[Category: Prutzman KC]]
-
[[Category: Schaller, M D.]]
+
[[Category: Schaller MD]]
-
[[Category: Fak]]
+
-
[[Category: Fat]]
+
-
[[Category: Focal adhension targeting domain]]
+
-
[[Category: Focal adhesion kinase]]
+
-
[[Category: Helix bundle]]
+
-
[[Category: Nmr]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 06:48:47 2009''
+

Current revision

SOLUTION STRUCTURE OF THE FAT DOMAIN OF FOCAL ADHESION KINASE

PDB ID 1qvx

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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