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1AFV

HIV-1 CAPSID PROTEIN (P24) COMPLEX WITH FAB25.3

1AFV の概要
エントリーDOI10.2210/pdb1afv/pdb
分子名称HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 CAPSID PROTEIN, ANTIBODY FAB25.3 FRAGMENT (LIGHT CHAIN), ANTIBODY FAB25.3 FRAGMENT (HEAVY CHAIN), ... (4 entities in total)
機能のキーワードcomplex (viral capsid-immunoglobulin), hiv, capsid protein, p24, viral protein-immune system complex, viral protein/immune system
由来する生物種Human immunodeficiency virus 1
詳細
細胞内の位置Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P12497
タンパク質・核酸の鎖数6
化学式量合計128732.14
構造登録者
主引用文献Momany, C.,Kovari, L.C.,Prongay, A.J.,Keller, W.,Gitti, R.K.,Lee, B.M.,Gorbalenya, A.E.,Tong, L.,McClure, J.,Ehrlich, L.S.,Summers, M.F.,Carter, C.,Rossmann, M.G.
Crystal structure of dimeric HIV-1 capsid protein.
Nat.Struct.Biol., 3:763-770, 1996
Cited by
PubMed Abstract: X-ray diffraction analysis of a human immunodeficiency virus (HIV-1) capsid (CA) protein shows that each monomer within the dimer consists of seven alpha-helices, five of which are arranged in a coiled coil-like structure. Sequence assignments were made for two of the helices, and tentative connectivity of the remainder of the protein was confirmed by the recent solution structure of a monomeric N-terminal fragment. The C-terminal third of the protein is mostly disordered in the crystal. The longest helices in the coiled coil-like structure are separated by a long, highly antigenic peptide that includes the binding site of an antibody fragment complexed with CA in the crystal. The site of binding of the Fab, the position of the antigenic loop and the site of cleavage between the matrix protein and CA establish the side of the dimer that would be on the exterior of the retroviral core.
PubMed: 8784350
DOI: 10.1038/nsb0996-763
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.7 Å)
構造検証レポート
Validation report summary of 1afv
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2026-02-04に公開中

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