4bcr

From Proteopedia

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m (Protected "4bcr" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4bcr| PDB=4bcr | SCENE= }}
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===Structure of PPARalpha in complex with WY14643===
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{{ABSTRACT_PUBMED_23707408}}
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The entry 4bcr is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/PPARA_HUMAN PPARA_HUMAN]] Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety (By similarity). Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2.<ref>PMID:7684926</ref> <ref>PMID:7629123</ref> <ref>PMID:9556573</ref> <ref>PMID:10195690</ref>
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Authors: Bernardes, A., Muniz, J.R.C., Polikarpov, I.
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==About this Structure==
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[[4bcr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BCR OCA].
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Description: Structure of PPARalpha in complex with WY14643
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==Reference==
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<ref group="xtra">PMID:023707408</ref><references group="xtra"/><references/>
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[[Category: Histone acetyltransferase]]
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[[Category: Homo sapiens]]
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[[Category: Bernardes, A.]]
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[[Category: Muniz, J R.C.]]
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[[Category: Polikarpov, I.]]
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[[Category: Fibrate]]
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[[Category: Nuclear receptor]]
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[[Category: Ppar]]
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[[Category: Transcription]]

Revision as of 13:27, 19 June 2013

Template:STRUCTURE 4bcr

Contents

Structure of PPARalpha in complex with WY14643

Template:ABSTRACT PUBMED 23707408

Function

[PPARA_HUMAN] Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety (By similarity). Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2.[1] [2] [3] [4]

About this Structure

4bcr is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Bernardes A, Souza PC, Muniz JR, Ricci CG, Ayers SD, Parekh NM, Godoy AS, Trivella DB, Reinach P, Webb P, Skaf MS, Polikarpov I. Molecular Mechanism of Peroxisome Proliferator-Activated Receptor alpha Activation by WY14643: a New Mode of Ligand Recognition and Receptor Stabilization. J Mol Biol. 2013 May 21. pii: S0022-2836(13)00309-4. doi:, 10.1016/j.jmb.2013.05.010. PMID:23707408 doi:10.1016/j.jmb.2013.05.010
  1. ↑ Sher T, Yi HF, McBride OW, Gonzalez FJ. cDNA cloning, chromosomal mapping, and functional characterization of the human peroxisome proliferator activated receptor. Biochemistry. 1993 Jun 1;32(21):5598-604. PMID:7684926
  2. ↑ Juge-Aubry CE, Gorla-Bajszczak A, Pernin A, Lemberger T, Wahli W, Burger AG, Meier CA. Peroxisome proliferator-activated receptor mediates cross-talk with thyroid hormone receptor by competition for retinoid X receptor. Possible role of a leucine zipper-like heptad repeat. J Biol Chem. 1995 Jul 28;270(30):18117-22. PMID:7629123
  3. ↑ Yan ZH, Karam WG, Staudinger JL, Medvedev A, Ghanayem BI, Jetten AM. Regulation of peroxisome proliferator-activated receptor alpha-induced transactivation by the nuclear orphan receptor TAK1/TR4. J Biol Chem. 1998 May 1;273(18):10948-57. PMID:9556573
  4. ↑ Gorla-Bajszczak A, Juge-Aubry C, Pernin A, Burger AG, Meier CA. Conserved amino acids in the ligand-binding and tau(i) domains of the peroxisome proliferator-activated receptor alpha are necessary for heterodimerization with RXR. Mol Cell Endocrinol. 1999 Jan 25;147(1-2):37-47. PMID:10195690

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