5lr7
From Proteopedia
(Difference between revisions)
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==CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR567530== | ==CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR567530== | ||
| - | <StructureSection load='5lr7' size='340' side='right' caption='[[5lr7]], [[Resolution|resolution]] 1.86Å' scene=''> | + | <StructureSection load='5lr7' size='340' side='right'caption='[[5lr7]], [[Resolution|resolution]] 1.86Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lr7]] 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=5LR7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LR7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5lr7]] 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=5LR7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LR7 FirstGlance]. <br> | ||
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== 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> | [[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> | ||
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| + | ==See Also== | ||
| + | *[[Heat Shock Proteins|Heat Shock Proteins]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Dupuy, A]] |
| + | [[Category: Vallee, F]] | ||
[[Category: Chaperone protein]] | [[Category: Chaperone protein]] | ||
Revision as of 06:01, 12 June 2019
CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR567530
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