3K4V

New crystal form of HIV-1 Protease/Saquinavir structure reveals carbamylation of N-terminal proline

3K4V の概要

• エントリーDOI: 10.2210/pdb3k4v/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000454
• 分子名称: HIV-1 Protease, DIMETHYL SULFOXIDE, (2S)-N-[(2S,3R)-4-[(2S,3S,4aS,8aS)-3-(tert-butylcarbamoyl)-3,4,4a,5,6,7,8,8a-octahydro-1H-isoquinolin-2-yl]-3-hydroxy-1 -phenyl-butan-2-yl]-2-(quinolin-2-ylcarbonylamino)butanediamide, ... (6 entities in total)
• 機能のキーワード: hydrolase-hydrolase inhibitor complex, carbamylation, aids, aspartyl protease, capsid maturation, capsid protein, hydrolase/hydrolase inhibitor
• 由来する生物種: Human immunodeficiency virus type 1 (HIV-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): P03366 P03366
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44706.43

構造登録者

Olajuyigbe, F.M.,Demitri, N.,Ajele, J.O.,Maurizio, E.,Randaccio, L.,Geremia, S. (登録日: 2009-10-06, 公開日: 2010-06-09, 最終更新日: 2023-09-06)

主引用文献

Olajuyigbe, F.M.,Demitri, N.,Ajele, J.O.,Maurizio, E.,Randaccio, L.,Geremia, S.
Carbamylation of N-terminal proline.
ACS Med Chem Lett, 1:254-257, 2010

PubMed Abstract: Protein carbamylation is of great concern both in vivo and in vitro. Here, we report the first structural characterization of a protein carbamylated at the N-terminal proline. The unexpected carbamylation of the α-amino group of the least reactive codified amino acid has been detected in high-resolution electron density maps of a new crystal form of the HIV-1 protease/saquinavir complex. The carbamyl group is found coplanar to the proline ring with a trans conformation. The reaction of N-terminal with cyanate ion derived from the chaotropic agent urea was confirmed by mass spectra analysis on protease single crystals. Implications of carbamylation process in vitro and in vivo are discussed.

PubMed: 24900204
DOI: 10.1021/ml100046d

実験手法

X-RAY DIFFRACTION (1.39 Å)