1zla
From Proteopedia
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| , resolution 2.9Å | |||||||
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| Ligands: | , , , | ||||||
| Gene: | Alpha-Satellite DNA (Homo sapiens), Histone H3 (Xenopus laevis), Histone H4 (Xenopus laevis), Histone H2A (other sequences), Histone H2B (Xenopus laevis) | ||||||
| Related: | 1aoi, 1f66, 1kx3, 1kx4, 1kx5
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Homo sapiens, Xenopus laevis and Other sequences. 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
Page seeded by OCA on Mon Mar 31 01:38:11 2008
