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Titolo:
The structure of a Michaelis serpin-protease complex
Autore:
Ye, S; Cech, AL; Belmares, R; Bergstrom, RC; Tong, YR; Corey, DR; Kanost, MR; Goldsmith, EJ;
Indirizzi:
Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 ed Ctr, Dept Biochem, Dallas, TX 75390 USA Univ Texas, SW Med Ctr, Dept Pharmacol, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 Ctr, Dept Pharmacol, Dallas, TX 75390 USA Kansas State Univ, Dept Biochem, Manhattan, KS 66506 USA Kansas State Univ Manhattan KS USA 66506 Biochem, Manhattan, KS 66506 USA
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 11, volume: 8, anno: 2001,
pagine: 979 - 983
SICI:
1072-8368(200111)8:11<979:TSOAMS>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMINOGEN-ACTIVATOR INHIBITOR-1; MOLECULAR REPLACEMENT; SERINE PROTEINASE; CRYSTAL-STRUCTURE; MANDUCA-SEXTA; CHYMOTRYPSIN; TRANSITION; VARIANT; RESIDUE; MUTANTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Goldsmith, EJ Univ Texas, SW Med Ctr, Dept Biochem, 5323 Harry Hines Blvd,Dallas, TX 75390 USA Univ Texas 5323 Harry Hines Blvd Dallas TX USA 75390 390 USA
Citazione:
S. Ye et al., "The structure of a Michaelis serpin-protease complex", NAT ST BIOL, 8(11), 2001, pp. 979-983

Abstract

Serine protease inhibitors (serpins) regulate the activities of circulating proteases. Serpins inhibit proteases by acylating the serine hydroxyl at their active sites. Before deacylation and complete proteolysis of the serpin can occur, massive conformational changes are triggered in the serpin while maintaining the covalent linkage between the protease and serpin. Here we report the structure of a serpin-trypsin Michaelis complex, which we visualized by using the S195A trypsin mutant to prevent covalent complex formation. This encounter complex reveals a more extensive interaction surface than that present in small inhibitor-protease complexes and is a template for modeling other serpin-protease pairs. Mutations of several serpin residues at the interface reduced the inhibitory activity of the serpin. The serine residue C-terminal to the scissile peptide bond is found in a closer thanusual interaction with His 57 at the active site of trypsin.

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Documento generato il 09/07/20 alle ore 01:36:53