4drp

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Current revision (14:43, 14 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4drp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DRP FirstGlance]. <br>
<table><tr><td colspan='2'>[[4drp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DRP FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0MD:{3-[(1R)-3-(3,4-DIMETHOXYPHENYL)-1-({[(2S)-1-{[(1R,2S)-2-ETHYL-1-HYDROXYCYCLOHEXYL](OXO)ACETYL}PIPERIDIN-2-YL]CARBONYL}OXY)PROPYL]PHENOXY}ACETIC+ACID'>0MD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0MD:{3-[(1R)-3-(3,4-DIMETHOXYPHENYL)-1-({[(2S)-1-{[(1R,2S)-2-ETHYL-1-HYDROXYCYCLOHEXYL](OXO)ACETYL}PIPERIDIN-2-YL]CARBONYL}OXY)PROPYL]PHENOXY}ACETIC+ACID'>0MD</scene></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=4drp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4drp OCA], [https://pdbe.org/4drp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4drp RCSB], [https://www.ebi.ac.uk/pdbsum/4drp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4drp ProSAT]</span></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=4drp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4drp OCA], [https://pdbe.org/4drp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4drp RCSB], [https://www.ebi.ac.uk/pdbsum/4drp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4drp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/FKBP5_HUMAN FKBP5_HUMAN]] Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP.
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[https://www.uniprot.org/uniprot/FKBP5_HUMAN FKBP5_HUMAN] Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The FK506-binding proteins (FKBP) 51 and 52 are cochaperones that modulate the signal transduction of steroid hormone receptors. Both proteins have been implicated in prostate cancer. Furthermore, single nucleotide polymorphisms in the gene encoding FKBP51 have been associated with a variety of psychiatric disorders. Rapamycin and FK506 are two macrocyclic natural products that bind to these proteins indiscriminately but with nanomolar affinity. We here report the cocrystal structure of FKBP51 with a simplified alpha-ketoamide analogue derived from FK506 and the first structure-activity relationship analysis for FKBP51 and FKBP52 based on this compound. In particular, the tert-pentyl group of this ligand was systematically replaced by a cyclohexyl ring system, which more closely resembles the pyranose ring in the high-affinity ligands rapamycin and FK506. The interaction with FKBPs was found to be surprisingly tolerant to the stereochemistry of the attached cyclohexyl substituents. The molecular basis for this tolerance was elucidated by X-ray cocrystallography.
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Evaluation of Synthetic FK506 Analogues as Ligands for the FK506-Binding Proteins 51 and 52.,Gopalakrishnan R, Kozany C, Gaali S, Kress C, Hoogeland B, Bracher A, Hausch F J Med Chem. 2012 May 10;55(9):4114-22. Epub 2012 Apr 19. PMID:22455444<ref>PMID:22455444</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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<div class="pdbe-citations 4drp" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[FKBP 3D structures|FKBP 3D structures]]
*[[FKBP 3D structures|FKBP 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Evaluation of Synthetic FK506 Analogs as Ligands for the FK506-Binding Proteins 51 and 52: Complex of FKBP51 with 2-(3-((R)-3-(3,4-dimethoxyphenyl)-1-((S)-1-(2-((1R,2S)-2-ethyl-1-hydroxy-cyclohexyl)-2-oxoacetyl)piperidine-2-carbonyloxy)propyl)phenoxy)acetic acid from cocrystallization

PDB ID 4drp

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