2v5w: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:2v5w.gif|left|200px]]<br /><applet load="2v5w" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2v5w.gif|left|200px]]
caption="2v5w, resolution 2.00&Aring;" />
 
'''CRYSTAL STRUCTURE OF HDAC8-SUBSTRATE COMPLEX'''<br />
{{Structure
|PDB= 2v5w |SIZE=350|CAPTION= <scene name='initialview01'>2v5w</scene>, resolution 2.00&Aring;
|SITE= <scene name='pdbsite=AC1:Mcm+Binding+Site+For+Chain+L'>AC1</scene>
|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=MCM:7-AMINO-4-METHYL-CHROMEN-2-ONE'>MCM</scene>
|ACTIVITY=
|GENE=
}}
 
'''CRYSTAL STRUCTURE OF HDAC8-SUBSTRATE COMPLEX'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
2V5W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=MCM:'>MCM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Mcm+Binding+Site+For+Chain+L'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5W OCA].  
2V5W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5W OCA].  


==Reference==
==Reference==
Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex., Vannini A, Volpari C, Gallinari P, Jones P, Mattu M, Carfi A, De Francesco R, Steinkuhler C, Di Marco S, EMBO Rep. 2007 Sep;8(9):879-84. Epub 2007 Aug 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17721440 17721440]
Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex., Vannini A, Volpari C, Gallinari P, Jones P, Mattu M, Carfi A, De Francesco R, Steinkuhler C, Di Marco S, EMBO Rep. 2007 Sep;8(9):879-84. Epub 2007 Aug 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17721440 17721440]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 42: Line 51:
[[Category: transcription regulation]]
[[Category: transcription regulation]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:53:21 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:43:21 2008''

Revision as of 16:43, 20 March 2008

File:2v5w.gif


Drag the structure with the mouse to rotate
2v5w, resolution 2.00Å
Sites: AC1
Ligands: K, ZN, ACE and MCM
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF HDAC8-SUBSTRATE COMPLEX


Overview

Histone deacetylases (HDACs)-an enzyme family that deacetylates histones and non-histone proteins-are implicated in human diseases such as cancer, and the first-generation of HDAC inhibitors are now in clinical trials. Here, we report the 2.0 A resolution crystal structure of a catalytically inactive HDAC8 active-site mutant, Tyr306Phe, bound to an acetylated peptidic substrate. The structure clarifies the role of active-site residues in the deacetylation reaction and substrate recognition. Notably, the structure shows the unexpected role of a conserved residue at the active-site rim, Asp 101, in positioning the substrate by directly interacting with the peptidic backbone and imposing a constrained cis-conformation. A similar interaction is observed in a new hydroxamate inhibitor-HDAC8 structure that we also solved. The crucial role of Asp 101 in substrate and inhibitor recognition was confirmed by activity and binding assays of wild-type HDAC8 and Asp101Ala, Tyr306Phe and Asp101Ala/Tyr306Phe mutants.

About this Structure

2V5W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex., Vannini A, Volpari C, Gallinari P, Jones P, Mattu M, Carfi A, De Francesco R, Steinkuhler C, Di Marco S, EMBO Rep. 2007 Sep;8(9):879-84. Epub 2007 Aug 10. PMID:17721440

Page seeded by OCA on Thu Mar 20 18:43:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2v5w&oldid=239590"