5lrz: Difference between revisions

Line 1:

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

~~The entry~~ 5lrz is ~~ON HOLD until Paper Publication~~

==CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH A003643501==

~~Authors~~: ~~VALLEE~~, F., ~~DUPUY~~, A.

== Structural highlights ==

<table><tr><td colspan='2'>[[5lrz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LRZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LRZ FirstGlance]. <br>

~~Description: CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH A003643501~~

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=73Y:6-bromanyl-~{N}-[(9~{R})-4-quinolin-3-yl-9~{H}-fluoren-9-yl]-3~{H}-imidazo[4,5-b]pyridine-7-carboxamide'>73Y</scene></td></tr>

[[~~Category~~: ~~Unreleased Structures~~]]

<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=5lrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lrz OCA], [http://pdbe.org/5lrz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lrz RCSB], [http://www.ebi.ac.uk/pdbsum/5lrz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lrz ProSAT]</span></td></tr>

[[Category: ~~Dupuy~~, A]]

</table>

[[Category: ~~Vallee~~, F]]

== 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>

== References ==

__TOC__

</StructureSection>

[[Category: DUPUY, A]]

[[Category: VALLEE, F]]

[[Category: Chaperone protein]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5lrz is ON HOLD  until Paper Publication
+==CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH A003643501==
+<StructureSection load='5lrz' size='340' side='right' caption='[[5lrz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-Authors: VALLEE, F., DUPUY, A.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5lrz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LRZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LRZ FirstGlance]. <br>
-Description: CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH A003643501
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=73Y:6-bromanyl-~{N}-[(9~{R})-4-quinolin-3-yl-9~{H}-fluoren-9-yl]-3~{H}-imidazo[4,5-b]pyridine-7-carboxamide'>73Y</scene></td></tr>
-[[Category: Unreleased Structures]]
+<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=5lrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lrz OCA], [http://pdbe.org/5lrz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lrz RCSB], [http://www.ebi.ac.uk/pdbsum/5lrz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lrz ProSAT]</span></td></tr>
-[[Category: Dupuy, A]]
+</table>
-[[Category: Vallee, F]]
+== 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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: DUPUY, A]]
+[[Category: VALLEE, F]]
+[[Category: Chaperone protein]]