1KJ4

SUBSTRATE SHAPE DETERMINES SPECIFICITY OF RECOGNITION RECOGNITION FOR HIV-1 PROTEASE: ANALYSIS OF CRYSTAL STRUCTURES OF SIX SUBSTRATE COMPLEXES

1KJ4 の概要

• エントリーDOI: 10.2210/pdb1kj4/pdb
• 関連するPDBエントリー: 1F7A 1KJ7 1KJF 1KJG 1KJH
• 分子名称: POL polyprotein, gag polyprotein, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: marix-capsid, substrate recognition, hydrolase
• 由来する生物種: Human immunodeficiency virus 1
• 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): P03369 P20875
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 46234.16

構造登録者

Schiffer, C.A. (登録日: 2001-12-04, 公開日: 2002-03-06, 最終更新日: 2023-08-16)

主引用文献

Prabu-Jeyabalan, M.,Nalivaika, E.,Schiffer, C.A.
Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes.
Structure, 10:369-381, 2002

PubMed Abstract: The homodimeric HIV-1 protease is the target of some of the most effective antiviral AIDS therapy, as it facilitates viral maturation by cleaving ten asymmetric and nonhomologous sequences in the Gag and Pol polyproteins. Since the specificity of this enzyme is not easily determined from the sequences of these cleavage sites alone, we solved the crystal structures of complexes of an inactive variant (D25N) of HIV-1 protease with six peptides that correspond to the natural substrate cleavage sites. When the protease binds to its substrate and buries nearly 1000 A2 of surface area, the symmetry of the protease is broken, yet most internal hydrogen bonds and waters are conserved. However, no substrate side chain hydrogen bond is conserved. Specificity of HIV-1 protease appears to be determined by an asymmetric shape rather than a particular amino acid sequence.

PubMed: 12005435
DOI: 10.1016/S0969-2126(02)00720-7

実験手法

X-RAY DIFFRACTION (2.9 Å)