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4RQS

Crystal structure of fully glycosylated HIV-1 gp120 core bound to CD4 and 17b Fab

4RQS の概要
エントリーDOI10.2210/pdb4rqs/pdb
分子名称2-domain CD4, 17b Fab Light Chain, 17b Fab Heavy Chain, ... (8 entities in total)
機能のキーワードimmunoglobulin fold, n-linked glycosylation, immune system
由来する生物種Homo sapiens (Human)
詳細
タンパク質・核酸の鎖数4
化学式量合計108437.06
構造登録者
Kong, L.,Wilson, I.A.,Kwong, P.D. (登録日: 2014-11-05, 公開日: 2014-12-31, 最終更新日: 2024-10-09)
主引用文献Kong, L.,Wilson, I.A.,Kwong, P.D.
Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262.
Proteins, 83:590-596, 2015
Cited by
PubMed Abstract: The crystal structure of a fully glycosylated HIV-1 gp120 core in complex with CD4 receptor and Fab 17b at 4.5-Å resolution reveals 9 of the 15 N-linked glycans of core gp120 to be partially ordered. The glycan at position Asn262 had the most extensive and well-ordered electron density, and a GlcNAc(2)Man(7) was modeled. The GlcNAc stem of this glycan is largely buried in a cleft in gp120, suggesting a role in gp120 folding and stability. Its arms interact with the stems of neighboring glycans from the oligomannose patch, which is a major target for broadly neutralizing antibodies.
PubMed: 25546301
DOI: 10.1002/prot.24747
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (4.493 Å)
構造検証レポート
Validation report summary of 4rqs
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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