2jv0

From Proteopedia

Revision as of 08:49, 23 January 2008

SET domain of RIZ1 tumor suppressor (PRDM2)

Overview

RIZ1 is a transcriptional regulator and tumor suppressor that catalyzes, methylation of lysine 9 of histone H3. It contains a distinct SET domain, sometimes referred to as PR (PRDI-BF1 and RIZ1 homology) domain, that is, responsible for its catalytic activity. We determined the solution, structure of the PR domain from RIZ1 and characterized its interaction, with S-adenosyl-l-homocysteine (SAH) and a peptide from histone H3., Despite low sequence identity with canonical SET domains, the PR domain, displays a typical SET fold including a pseudo-knot at the C-terminus. The, N-flanking sequence of RIZ1 PR domain adopts a novel conformation and, interacts closely with the SET fold. The C-flanking sequence contains an, alpha-helix that points away from the protein face that harbors active, site in other SET domains. The SET fold of RIZ1 does not have detectable, affinity for SAH but it interacts with a synthetic peptide comprising, residues 1-20 of histone H3.

About this Structure

2JV0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural studies of the SET domain from RIZ1 tumor suppressor., Briknarova K, Zhou X, Satterthwait A, Hoyt DW, Ely KR, Huang S, Biochem Biophys Res Commun. 2008 Feb 15;366(3):807-13. Epub 2007 Dec 17. PMID:18082620

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