View source for 4l90


==Crystal structure of Human Hsp90 with RL3==
<StructureSection load='4l90' size='340' side='right'caption='[[4l90]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4l90]] 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=4L90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L90 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RL3:[5-(6-BROMO[1,2,4]TRIAZOLO[4,3-A]PYRIDIN-3-YL)-2,4-DIHYDROXYPHENYL](4-METHYLPIPERAZIN-1-YL)METHANONE'>RL3</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l8z|4l8z]], [[4l91|4l91]], [[4l93|4l93]], [[4l94|4l94]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1 ([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=4l90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l90 OCA], [http://pdbe.org/4l90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l90 RCSB], [http://www.ebi.ac.uk/pdbsum/4l90 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l90 ProSAT]</span></td></tr>
</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>  

==See Also==
*[[Heat Shock Proteins|Heat Shock Proteins]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: He, J]]
[[Category: Li, J]]
[[Category: Ren, J]]
[[Category: Xiong, B]]
[[Category: Yang, M]]
[[Category: Atp hydrolysis]]
[[Category: Chaperone-chaperone inhibitor complex]]
[[Category: Hsp90n-hsp90n inhibitor complex]]