21fe: Difference between revisions
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New page: '''Unreleased structure''' The entry 21fe is ON HOLD Authors: Hirano, Y., Kusaka, K., Ose, T., Kurihara, K., Aburai, K., Saito, J., Tamata, T. Description: Neutron crystal structure of... |
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==Neutron crystal structure of the ADP bound form of the human Hsp90 N-terminal domain== | |||
<StructureSection load='21fe' size='340' side='right'caption='[[21fe]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[21fe]] 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=21FE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=21FE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Neutron Diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=21fe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=21fe OCA], [https://pdbe.org/21fe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=21fe RCSB], [https://www.ebi.ac.uk/pdbsum/21fe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=21fe ProSAT]</span></td></tr> | ||
[[Category: Hirano | </table> | ||
[[Category: | == Function == | ||
[[Category: Kusaka | [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> | ||
[[Category: Ose | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Aburai K]] | |||
[[Category: Hirano Y]] | |||
[[Category: Kurihara K]] | |||
[[Category: Kusaka K]] | |||
[[Category: Ose T]] | |||
[[Category: Saito J]] | |||
[[Category: Tamada T]] | |||
Latest revision as of 06:35, 3 June 2026
Neutron crystal structure of the ADP bound form of the human Hsp90 N-terminal domain
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