1uz3: Difference between revisions

Revision as of 02:54, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1uz3.png

Template:STRUCTURE 1uz3

CRYSTAL STRUCTURE OF NOVEL PROTEIN EMSYCRYSTAL STRUCTURE OF NOVEL PROTEIN EMSY

Template:ABSTRACT PUBMED 15978617

About this StructureAbout this Structure

1UZ3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the ENT domain of human EMSY., Chavali GB, Ekblad CM, Basu BP, Brissett NC, Veprintsev D, Hughes-Davies L, Kouzarides T, Itzhaki LS, Doherty AJ, J Mol Biol. 2005 Jul 29;350(5):964-73. PMID:15978617

Page seeded by OCA on Mon Jul 28 02:54:12 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1uz3.gif|left|200px]]
+{{Seed}}
+[[Image:1uz3.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1uz3|  PDB=1uz3  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF NOVEL PROTEIN EMSY'''
+===CRYSTAL STRUCTURE OF NOVEL PROTEIN EMSY===
-==Overview==
+<!--
-EMSY is a recently discovered gene encoding a BRCA2-associated protein and is amplified in some sporadic breast and ovarian cancers. The EMSY sequence contains no known domain except for a conserved approximately 100 residue segment at the N terminus. This so-called ENT domain is unique in the human genome, although multiple copies are found in Arabidopsis proteins containing members of the Royal family of chromatin remodelling domains. Here, we report the crystal structure of the ENT domain of EMSY, consisting of a unique arrangement of five alpha-helices that fold into a helical bundle arrangement. The fold shares regions of structural homology with the DNA-binding domain of homeodomain proteins. The ENT domain forms a homodimer via the anti-parallel packing of the extended N-terminal alpha-helix of each molecule. It is stabilized mainly by hydrophobic residues at the dimer interface and has a dissociation constant in the low micromolar range. The dimerisation of EMSY mediated by the ENT domain could provide flexibility for it to bind two or more different substrates simultaneously.
+The line below this paragraph, {{ABSTRACT_PUBMED_15978617}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15978617 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15978617}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Chromatin regulator]]
 [[Category: Royal family domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:53:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:54:12 2008''