2fo6
From Proteopedia
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{{Theoretical_model}} | {{Theoretical_model}} | ||
- | + | ==3D MODEL OF A TRUNCATED HUMAN PYK2 FERM DOMAIN== | |
- | + | <StructureSection load='2fo6' size='340' side='right'caption='[[2fo6]]' 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=2FO6 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=2fo6 FirstGlance], [https://www.ebi.ac.uk/pdbsum/2fo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fo6 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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> | |
- | <ref | + | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 2fo6" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Theoretical Model]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Dooley, A J]] | [[Category: Dooley, A J]] | ||
[[Category: Pang, Y-P]] | [[Category: Pang, Y-P]] |
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
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