1j8f
From Proteopedia
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HUMAN SIRT2 HISTONE DEACETYLASE
Overview
Sir2 is an NAD-dependent histone deacetylase that mediates transcriptional silencing at mating-type loci, telomeres and ribosomal gene clusters, and has a critical role in the determination of life span in yeast and Caenorhabditis elegans. The 1.7 A crystal structure of the 323 amino acid catalytic core of human SIRT2, a homolog of yeast Sir2, reveals an NAD-binding domain, which is a variant of the Rossmann fold, and a smaller domain composed of a helical module and a zinc-binding module. A conserved large groove at the interface of the two domains is the likely site of catalysis based on mutagenesis. Intersecting this large groove, there is a pocket formed by the helical module. The pocket is lined with hydrophobic residues conserved within each of the five Sir2 classes, suggesting that it is a class-specific protein-binding site.
About this Structure
1J8F is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the histone deacetylase SIRT2., Finnin MS, Donigian JR, Pavletich NP, Nat Struct Biol. 2001 Jul;8(7):621-5. PMID:11427894
Page seeded by OCA on Thu Feb 21 13:19:49 2008
