3tuh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal Structure of the N-terminal domain of an HSP90 in the presence of an the inhibitor ganetespib==
==Crystal Structure of the N-terminal domain of an HSP90 in the presence of an the inhibitor ganetespib==
-
<StructureSection load='3tuh' size='340' side='right' caption='[[3tuh]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+
<StructureSection load='3tuh' size='340' side='right'caption='[[3tuh]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3tuh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TUH FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3tuh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TUH FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TUH:5-[2,4-DIHYDROXY-5-(PROPAN-2-YL)PHENYL]-4-(1-METHYL-1H-INDOL-5-YL)-2,4-DIHYDRO-3H-1,2,4-TRIAZOL-3-ONE'>TUH</scene></td></tr>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TUH:5-[2,4-DIHYDROXY-5-(PROPAN-2-YL)PHENYL]-4-(1-METHYL-1H-INDOL-5-YL)-2,4-DIHYDRO-3H-1,2,4-TRIAZOL-3-ONE'>TUH</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-
<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=3tuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tuh OCA], [http://pdbe.org/3tuh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tuh RCSB], [http://www.ebi.ac.uk/pdbsum/3tuh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tuh ProSAT]</span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tuh OCA], [https://pdbe.org/3tuh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tuh RCSB], [https://www.ebi.ac.uk/pdbsum/3tuh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tuh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
+
[[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>
==See Also==
==See Also==
-
*[[Heat Shock Proteins|Heat Shock Proteins]]
+
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
Line 18: Line 18:
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
 +
[[Category: Large Structures]]
[[Category: Ying, W]]
[[Category: Ying, W]]
[[Category: Atp binding]]
[[Category: Atp binding]]
[[Category: Chaperone protein]]
[[Category: Chaperone protein]]
[[Category: Chaperone-inhibitor complex]]
[[Category: Chaperone-inhibitor complex]]

Revision as of 13:40, 17 November 2021

Crystal Structure of the N-terminal domain of an HSP90 in the presence of an the inhibitor ganetespib

PDB ID 3tuh

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools