9imw: Difference between revisions

Line 1:

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

~~The entry~~ 9imw is ~~ON HOLD until Paper Publication~~

==Crystal structure of N-terminal domain of human Hsp90==

~~Authors~~: ~~Huang~~, L.Q., Yu, F.

== Structural highlights ==

<table><tr><td colspan='2'>[[9imw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9IMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9IMW FirstGlance]. <br>

~~Description~~: ~~Crystal structure~~ of N-~~terminal domain of human Hsp90~~

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.527Å</td></tr>

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

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9imw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9imw OCA], [https://pdbe.org/9imw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9imw RCSB], [https://www.ebi.ac.uk/pdbsum/9imw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9imw ProSAT]</span></td></tr>

[[Category: Huang~~, L.Q~~]]

</table>

[[Category: Yu, F]]

== Function ==

[https://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: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Huang LQ]]

[[Category: Yu F]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9imw is ON HOLD  until Paper Publication
+==Crystal structure of N-terminal domain of human Hsp90==
+<StructureSection load='9imw' size='340' side='right'caption='[[9imw]], [[Resolution|resolution]] 1.53&Aring;' scene=''>
-Authors: Huang, L.Q., Yu, F.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9imw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9IMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9IMW FirstGlance]. <br>
-Description: Crystal structure of N-terminal domain of human Hsp90
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.527&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9imw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9imw OCA], [https://pdbe.org/9imw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9imw RCSB], [https://www.ebi.ac.uk/pdbsum/9imw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9imw ProSAT]</span></td></tr>
-[[Category: Huang, L.Q]]
+</table>
-[[Category: Yu, F]]
+== Function ==
+[https://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: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Huang LQ]]
+[[Category: Yu F]]