2l4s: Difference between revisions
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==Promiscuous Binding at the Crossroads of Numerous Cancer Pathways: Insight from the Binding of GIP with Glutaminase L== | |||
<StructureSection load='2l4s' size='340' side='right' caption='[[2l4s]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2l4s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L4S FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2l4t|2l4t]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TAX1BP3, TIP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l4s RCSB], [http://www.ebi.ac.uk/pdbsum/2l4s PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glutaminase Interacting Protein (GIP) is composed of a single PDZ domain that interacts with a growing list of partner proteins, including Glutaminase L, that are involved in a number of cell signaling and cancer pathways. Therefore, GIP makes a good target for structure-based drug design. Here we report the solution structures of both free GIP and GIP bound to the C-terminal peptide analog of Glutaminase L. This is the first reported NMR structure of GIP in a complex with one of its binding partners. Our analysis of both free GIP and GIP complexed with the Glutaminase L peptide provides important insights into how a promiscuous binding domain can have affinity for multiple binding partners. Through a detailed chemical shift perturbation analysis and backbone dynamics studies, we demonstrate here that the binding of the Glutaminase L peptide to GIP is an allosteric event. Taken together, the insights reported here lay the groundwork for the future development of a specific inhibitor for GIP. | |||
Promiscuous Binding at the Crossroads of Numerous Cancer Pathways: Insight from the Binding of GIP with Glutaminase L.,Zoetewey DL, Ovee M, Banerjee M, Bhaskaran R, Mohanty S Biochemistry. 2011 Mar 18. PMID:21417405<ref>PMID:21417405</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Banerjee, M | [[Category: Banerjee, M]] | ||
[[Category: Bhaskaran, R | [[Category: Bhaskaran, R]] | ||
[[Category: Mohanty, S | [[Category: Mohanty, S]] | ||
[[Category: Ovee, M | [[Category: Ovee, M]] | ||
[[Category: Zoetewey, D L | [[Category: Zoetewey, D L]] | ||
[[Category: Gip]] | [[Category: Gip]] | ||
[[Category: Glutatminase l]] | [[Category: Glutatminase l]] | ||
[[Category: Pdz domain]] | [[Category: Pdz domain]] | ||
[[Category: Peptide binding protein]] | [[Category: Peptide binding protein]] | ||
