1zla

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Revision as of 05:23, 21 November 2007

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spinqualitylabelsall models 1zla, resolution 2.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-ray Structure of a Kaposi's sarcoma herpesvirus LANA peptide bound to the nucleosomal core

Overview

Kaposi's sarcoma-associated herpesvirus (KSHV) latency-associated nuclear, antigen (LANA) mediates viral genome attachment to mitotic chromosomes. We, find that N-terminal LANA docks onto chromosomes by binding nucleosomes, through the folded region of histones H2A-H2B. The same LANA residues were, required for both H2A-H2B binding and chromosome association. Further, LANA did not bind Xenopus sperm chromatin, which is deficient in H2A-H2B;, chromatin binding was rescued after assembly of nucleosomes containing, H2A-H2B. We also describe the 2.9-angstrom crystal structure of a, nucleosome complexed with the first 23 LANA amino acids. The LANA peptide, forms a hairpin that interacts exclusively with an acidic H2A-H2B region, that is implicated in the formation of higher order chromatin structure., Our findings present a paradigm for how nucleosomes may serve as binding, platforms for viral and cellular proteins and reveal a previously unknown, mechanism for KSHV latency.

About this Structure

1ZLA is a Protein complex structure of sequences from Expression vector pcy215, Homo sapiens and Xenopus laevis. Full crystallographic information is available from OCA.

Reference

The nucleosomal surface as a docking station for Kaposi's sarcoma herpesvirus LANA., Barbera AJ, Chodaparambil JV, Kelley-Clarke B, Joukov V, Walter JC, Luger K, Kaye KM, Science. 2006 Feb 10;311(5762):856-61. PMID:16469929

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