4hy6: Difference between revisions

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~~'''Unreleased structure'''~~

===Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ1===

~~The entry 4hy6~~ is ~~ON HOLD~~ ~~until May 13 2014~~

==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>

~~Authors~~: ~~Yang, M~~.~~, Li, J~~.~~, He, J~~.H.

==About this Structure==

[[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].

~~Description~~: ~~Crystal Structure of the human Hsp90~~-~~alpha N-domain bound to the hsp90~~ inhibitor ~~FJ1~~

==Reference==

[[Category: Homo sapiens]]

[[Category: He, J H.]]

[[Category: Li, J.]]

[[Category: Yang, M.]]

[[Category: Atp binding]]

[[Category: Atp hydrolysis]]

[[Category: Chaperone-chaperone inhibitor complex]]

[[Category: Inhibitor]]

[[Category: Molecular chaperone]]

[[Category: Molecularchaperone]]

[[Category: Rossmann fold]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{STRUCTURE_4hy6|  PDB=4hy6  |  SCENE=  }}
+===Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ1===
-The entry 4hy6 is ON HOLD  until May 13 2014
+==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>
-Authors: Yang, M., Li, J., He, J.H.
+==About this Structure==
+[[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].
-Description: Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ1
+==Reference==
+<references group="xtra"/><references/>
+[[Category: Homo sapiens]]
+[[Category: He, J H.]]
+[[Category: Li, J.]]
+[[Category: Yang, M.]]
+[[Category: Atp binding]]
+[[Category: Atp hydrolysis]]
+[[Category: Chaperone-chaperone inhibitor complex]]
+[[Category: Inhibitor]]
+[[Category: Molecular chaperone]]
+[[Category: Molecularchaperone]]
+[[Category: Rossmann fold]]