5lq9: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
Line 1: Line 1:


==CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR200323.==
==CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR200323.==
<StructureSection load='5lq9' size='340' side='right' caption='[[5lq9]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='5lq9' size='340' side='right'caption='[[5lq9]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5lq9]] 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=5LQ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LQ9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5lq9]] 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=5LQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LQ9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=72K:4-(3-methyl-4-quinolin-3-yl-indazol-1-yl)-2-[(4-oxidanylcyclohexyl)amino]benzamide'>72K</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=72K:4-(3-methyl-4-quinolin-3-yl-indazol-1-yl)-2-[(4-oxidanylcyclohexyl)amino]benzamide'>72K</scene></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=5lq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lq9 OCA], [http://pdbe.org/5lq9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lq9 RCSB], [http://www.ebi.ac.uk/pdbsum/5lq9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lq9 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=5lq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lq9 OCA], [https://pdbe.org/5lq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lq9 RCSB], [https://www.ebi.ac.uk/pdbsum/5lq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lq9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[https://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 Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Dupuy, A]]
[[Category: Large Structures]]
[[Category: Vallee, F]]
[[Category: Dupuy A]]
[[Category: Chaperone protein]]
[[Category: Vallee F]]

Latest revision as of 18:41, 18 October 2023

CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR200323.

5lq9, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA