4K2J

Decameric ring structure of KSHV (HHV-8) latency-associated nuclear antigen (LANA) DNA binding domain

4K2J の概要

• エントリーDOI: 10.2210/pdb4k2j/pdb
• 分子名称: KSHV (HHV-8) latency-associated nuclear antigen (LANA), FORMIC ACID, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: dna binding, dna binding protein, viral protein
• 由来する生物種: Human herpesvirus 8 (HHV-8)
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 160613.77

構造登録者

Domsic, J.F.,Marmorstein, R. (登録日: 2013-04-09, 公開日: 2013-11-06, 最終更新日: 2024-02-28)

主引用文献

Domsic, J.F.,Chen, H.S.,Lu, F.,Marmorstein, R.,Lieberman, P.M.
Molecular Basis for Oligomeric-DNA Binding and Episome Maintenance by KSHV LANA.
Plos Pathog., 9:e1003672-e1003672, 2013

PubMed Abstract: LANA is the KSHV-encoded terminal repeat binding protein essential for viral replication and episome maintenance during latency. We have determined the X-ray crystal structure of LANA C-terminal DNA binding domain (LANADBD) to reveal its capacity to form a decameric ring with an exterior DNA binding surface. The dimeric core is structurally similar to EBV EBNA1 with an N-terminal arm that regulates DNA binding and is required for replication function. The oligomeric interface between LANA dimers is dispensable for single site DNA binding, but is required for cooperative DNA binding, replication function, and episome maintenance. We also identify a basic patch opposite of the DNA binding surface that is responsible for the interaction with BRD proteins and contributes to episome maintenance function. The structural features of LANADBD suggest a novel mechanism of episome maintenance through DNA-binding induced oligomeric assembly.

PubMed: 24146617
DOI: 10.1371/journal.ppat.1003672

実験手法

X-RAY DIFFRACTION (2.05 Å)