2fo6

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:2fo6.png|left|200px]]
 
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==3D MODEL OF A TRUNCATED HUMAN PYK2 FERM DOMAIN==
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The line below this paragraph, containing "STRUCTURE_2fo6", creates the "Structure Box" on the page.
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<StructureSection load='2fo6' size='340' side='right'caption='[[2fo6]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FO6 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=2fo6 FirstGlance], [https://www.ebi.ac.uk/pdbsum/2fo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fo6 ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_2fo6| PDB=2fo6 | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The strong tendency of malignant glioma cells to invade locally into surrounding normal brain precludes effective surgical resection, reduces the efficacy of radiotherapy, and is associated with increased resistance to chemotherapy regimens. We report that the N-terminal FERM domain of Pyk2 regulates its promigratory function. A 3-dimensional model of the Pyk2 FERM domain was generated and mutagenesis studies identified residues essential for Pyk2 promigratory function. Model-based targeted mutations within the FERM domain decreased Pyk2 phosphorylation and reduced the capacity of Pyk2 to stimulate glioma cell migration but did not significantly alter the intracellular distribution of Pyk2. Expression of autonomous Pyk2 FERM domain fragments containing analogous mutations exhibited reduced capacity to inhibit glioma cell migration and Pyk2 phosphorylation relative to expression of an autonomous wild type FERM domain fragment. These results indicate that the FERM domain plays an important role in regulating the functional competency of Pyk2 as a promigratory factor in glioma.
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===3D MODEL OF A TRUNCATED HUMAN PYK2 FERM DOMAIN===
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Critical role of the FERM domain in Pyk2 stimulated glioma cell migration.,Lipinski CA, Tran NL, Dooley A, Pang YP, Rohl C, Kloss J, Yang Z, McDonough W, Craig D, Berens ME, Loftus JC Biochem Biophys Res Commun. 2006 Oct 27;349(3):939-47. Epub 2006 Aug 31. PMID:16962067<ref>PMID:16962067</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16962067}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2fo6" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16962067 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16962067}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FO6 OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:16962067</ref><references group="xtra"/>
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[[Category: Dooley, A J]]
[[Category: Dooley, A J]]
[[Category: Pang, Y-P]]
[[Category: Pang, Y-P]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 07:49:14 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

3D MODEL OF A TRUNCATED HUMAN PYK2 FERM DOMAIN

PDB ID 2fo6

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