5lnz: Difference between revisions

Line 1:

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

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

==HSP90 WITH indazole derivative==

~~Authors~~: ~~Graedler~~, U., ~~Amaral~~, M., ~~Schuetz~~, D.

== Structural highlights ==

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

~~Description~~: ~~HSP90 WITH indazole derivative~~

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=70Z:~{N}3-butyl-~{N}3,~{N}5-dimethyl-~{N}5-(4-morpholin-4-ylphenyl)-6-oxidanyl-2~{H}-indazole-3,5-dicarboxamide'>70Z</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=5lnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lnz OCA], [http://pdbe.org/5lnz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lnz RCSB], [http://www.ebi.ac.uk/pdbsum/5lnz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lnz ProSAT]</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>

== References ==

__TOC__

</StructureSection>

[[Category: Amaral, M]]

[[Category: Graedler, U]]

[[Category: Schuetz, D]]

[[Category: ~~Graedler, U]]~~

[[Category: Chaperone]]

~~[[Category: Amaral, M~~]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5lnz is ON HOLD  until Paper Publication
+==HSP90 WITH indazole derivative==
+<StructureSection load='5lnz' size='340' side='right' caption='[[5lnz]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
-Authors: Graedler, U., Amaral, M., Schuetz, D.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5lnz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LNZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LNZ FirstGlance]. <br>
-Description: HSP90 WITH indazole derivative
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=70Z:~{N}3-butyl-~{N}3,~{N}5-dimethyl-~{N}5-(4-morpholin-4-ylphenyl)-6-oxidanyl-2~{H}-indazole-3,5-dicarboxamide'>70Z</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=5lnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lnz OCA], [http://pdbe.org/5lnz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lnz RCSB], [http://www.ebi.ac.uk/pdbsum/5lnz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lnz ProSAT]</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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Amaral, M]]
+[[Category: Graedler, U]]
 [[Category: Schuetz, D]]
-[[Category: Graedler, U]]
+[[Category: Chaperone]]
-[[Category: Amaral, M]]