1ZLA

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

Summary for 1ZLA

• Entry DOI: 10.2210/pdb1zla/pdb
• Related: 1aoi 1f66 1kx3 1kx4 1kx5
• Descriptor: Palindromic 146bp Human alpha-Satellite DNA fragment, histone H3, Histone H4, ... (7 entities in total)
• Functional Keywords: latency associated nuclear antigen (lana), kaposi's sarcoma herpes virus (kshv), nucleosome core particle, chromatin, protein/protein interaction, structural protein-dna complex, structural protein/dna
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 11
• Total formula weight: 201529.63

Authors

Chodaparambil, J.V.,Barbera, A.J.,Kaye, K.M.,Luger, K. (deposition date: 2005-05-05, release date: 2006-02-28, Last modification date: 2023-08-23)

Primary citation

Barbera, A.J.,Chodaparambil, J.V.,Kelley-Clarke, B.,Joukov, V.,Walter, J.C.,Luger, K.,Kaye, K.M.
The nucleosomal surface as a docking station for Kaposi's sarcoma herpesvirus LANA.
Science, 311:856-861, 2006

PubMed Abstract: 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.

PubMed: 16469929
DOI: 10.1126/science.1120541

Experimental method

X-RAY DIFFRACTION (2.9 Å)