5ls1: Difference between revisions

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'''Unreleased structure'''


The entry 5ls1 is ON HOLD  until Paper Publication
==CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR166475==
 
<StructureSection load='5ls1' size='340' side='right' caption='[[5ls1]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
Authors: VALLEE, F., DUPUY, A.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5ls1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LS1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LS1 FirstGlance]. <br>
Description: CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR166475
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=73Z:2-[(4-oxidanylidenecyclohexyl)amino]-4-(3,6,6-trimethyl-4-oxidanylidene-5,7-dihydroindol-1-yl)benzamide'>73Z</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
[[Category: Dupuy, A]]
<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=5ls1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ls1 OCA], [http://pdbe.org/5ls1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ls1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ls1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ls1 ProSAT]</span></td></tr>
[[Category: Vallee, F]]
</table>
== Function ==
[[http://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: DUPUY, A]]
[[Category: VALLEE, F]]
[[Category: Chaperone protein]]

Revision as of 04:43, 16 November 2017

CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR166475CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR166475

Structural highlights

5ls1 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:HSP90AA1, HSP90A, HSPC1, HSPCA (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.[1] [2]

References

  1. ↑ Martinez-Ruiz A, Villanueva L, Gonzalez de Orduna C, Lopez-Ferrer D, Higueras MA, Tarin C, Rodriguez-Crespo I, Vazquez J, Lamas S. S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc Natl Acad Sci U S A. 2005 Jun 14;102(24):8525-30. Epub 2005 Jun 3. PMID:15937123 doi:10.1073/pnas.0407294102
  2. ↑ Forsythe HL, Jarvis JL, Turner JW, Elmore LW, Holt SE. Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. J Biol Chem. 2001 May 11;276(19):15571-4. Epub 2001 Mar 23. PMID:11274138 doi:10.1074/jbc.C100055200

5ls1, resolution 1.85Å

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