4hy6: Difference between revisions
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==Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ1== | |||
<StructureSection load='4hy6' size='340' side='right' caption='[[4hy6]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
==Function== | <table><tr><td colspan='2'>[[4hy6]] is a 1 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=4HY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HY6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FJ1:6,6-DIMETHYL-3-(TRIFLUOROMETHYL)-1,5,6,7-TETRAHYDRO-4H-INDAZOL-4-ONE'>FJ1</scene></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 Homo sapiens])</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=4hy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hy6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hy6 RCSB], [http://www.ebi.ac.uk/pdbsum/4hy6 PDBsum]</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> | [[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/> | ||
<references | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: He, J H | [[Category: He, J H]] | ||
[[Category: Li, J | [[Category: Li, J]] | ||
[[Category: Yang, M | [[Category: Yang, M]] | ||
[[Category: Atp binding]] | [[Category: Atp binding]] | ||
[[Category: Atp hydrolysis]] | [[Category: Atp hydrolysis]] | ||
