5xrb: Difference between revisions

Revision as of 10:06, 4 July 2018

Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ5Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ5

Structural highlights

5xrb is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

References

↑ Martinez-Ruiz A, Villanueva L, Gonzalez de Orduna C, Lopez-Ferrer D, Higueras MA, Tarin C, Rodriguez-Crespo I, Vazquez J, Lamas S. S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc Natl Acad Sci U S A. 2005 Jun 14;102(24):8525-30. Epub 2005 Jun 3. PMID:15937123 doi:10.1073/pnas.0407294102
↑ Forsythe HL, Jarvis JL, Turner JW, Elmore LW, Holt SE. Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. J Biol Chem. 2001 May 11;276(19):15571-4. Epub 2001 Mar 23. PMID:11274138 doi:10.1074/jbc.C100055200

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Martinez-Ruiz A, Villanueva L, Gonzalez de Orduna C, Lopez-Ferrer D, Higueras MA, Tarin C, Rodriguez-Crespo I, Vazquez J, Lamas S. S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc Natl Acad Sci U S A. 2005 Jun 14;102(24):8525-30. Epub 2005 Jun 3. PMID:15937123 doi:10.1073/pnas.0407294102

[2] Forsythe HL, Jarvis JL, Turner JW, Elmore LW, Holt SE. Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. J Biol Chem. 2001 May 11;276(19):15571-4. Epub 2001 Mar 23. PMID:11274138 doi:10.1074/jbc.C100055200

[1]

[2]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5xrb is ON HOLD  until Paper Publication
+==Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ5==
+<StructureSection load='5xrb' size='340' side='right' caption='[[5xrb]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
-Authors: Li, J., Shi, F., Xiong, B., He, J.H.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5xrb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XRB FirstGlance]. <br>
-Description: Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ5
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8DU:N-[3-[5-chloranyl-2,4-bis(oxidanyl)phenyl]-4-(4-methoxyphenyl)-1,2-oxazol-5-yl]cyclopropanecarboxamide'>8DU</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=5xrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xrb OCA], [http://pdbe.org/5xrb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xrb RCSB], [http://www.ebi.ac.uk/pdbsum/5xrb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xrb 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: He, J H]]
 [[Category: Li, J]]
 [[Category: Shi, F]]
 [[Category: Xiong, B]]
-[[Category: He, J.H]]
+[[Category: Chaperone]]
+[[Category: Complex]]
+[[Category: Heat shock protein hsp 90]]
+[[Category: Inhibitor]]

5xrb: Difference between revisions

Revision as of 10:06, 4 July 2018

Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ5Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ5

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

5xrb: Difference between revisions

Revision as of 10:06, 4 July 2018

Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ5Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ5

Structural highlights

Function

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Search