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2l4s

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Revision as of 19:52, 1 August 2018

Promiscuous Binding at the Crossroads of Numerous Cancer Pathways: Insight from the Binding of GIP with Glutaminase L

Structural highlights

2l4s is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2l4t
Gene:	TAX1BP3, TIP1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TX1B3_HUMAN] May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway. May play a role in activation of CDC42 by the viral protein HPV16 E6.^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Reynaud C, Fabre S, Jalinot P. The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element. J Biol Chem. 2000 Oct 27;275(43):33962-8. PMID:10940294 doi:10.1074/jbc.M000465200
↑ Alewine C, Olsen O, Wade JB, Welling PA. TIP-1 has PDZ scaffold antagonist activity. Mol Biol Cell. 2006 Oct;17(10):4200-11. Epub 2006 Jul 19. PMID:16855024 doi:10.1091/mbc.E06-02-0129
↑ Oliver AW, He X, Borthwick K, Donne AJ, Hampson L, Hampson IN. The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which activates Cdc42. Br J Cancer. 2011 Jan 18;104(2):324-31. doi: 10.1038/sj.bjc.6606026. Epub 2010, Dec 7. PMID:21139582 doi:10.1038/sj.bjc.6606026
↑ Zoetewey DL, Ovee M, Banerjee M, Bhaskaran R, Mohanty S. Promiscuous Binding at the Crossroads of Numerous Cancer Pathways: Insight from the Binding of GIP with Glutaminase L. Biochemistry. 2011 Mar 18. PMID:21417405 doi:10.1021/bi102055y

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l4s"

@@ Line 1: / Line 1: @@
 ==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=''>
@@ Line 5: / Line 6: @@
 </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 HUMAN])</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://pdbe.org/2l4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l4s RCSB], [http://www.ebi.ac.uk/pdbsum/2l4s PDBsum]</span></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://pdbe.org/2l4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l4s RCSB], [http://www.ebi.ac.uk/pdbsum/2l4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l4s ProSAT]</span></td></tr>
 </table>
 == Function ==

2l4s

From Proteopedia

Revision as of 19:52, 1 August 2018

Promiscuous Binding at the Crossroads of Numerous Cancer Pathways: Insight from the Binding of GIP with Glutaminase L

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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