1yer
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1yer]] 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=1YER OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YER FirstGlance]. <br> | <table><tr><td colspan='2'>[[1yer]] 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=1YER OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YER FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yer OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yer RCSB], [http://www.ebi.ac.uk/pdbsum/1yer PDBsum]</span></td></tr> | + | </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=1yer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yer OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yer RCSB], [http://www.ebi.ac.uk/pdbsum/1yer PDBsum]</span></td></tr> |
| - | <table> | + | </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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Pavletich, N P | + | [[Category: Pavletich, N P]] |
| - | [[Category: Russo, A A | + | [[Category: Russo, A A]] |
| - | [[Category: Stebbins, C E | + | [[Category: Stebbins, C E]] |
[[Category: Chaperone protein]] | [[Category: Chaperone protein]] | ||
[[Category: Geldanamycin]] | [[Category: Geldanamycin]] | ||
[[Category: Heat shock]] | [[Category: Heat shock]] | ||
[[Category: Signal transduction]] | [[Category: Signal transduction]] | ||
Revision as of 20:31, 25 December 2014
HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "CLOSED" CONFORMATION
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