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Titolo:
Binding diversity of a noncovalent-type low-molecular-weight serine protease inhibitor and function of a catalytic water molecule: X-ray crystal structure of PKSI-527-inhibited trypsin
Autore:
Tomoo, K; Satoh, K; Tsuda, Y; Wanaka, K; Okamoto, S; Hijikata-Okunomiya, A; Okada, Y; Ishida, T;
Indirizzi:
Osaka Univ Pharmaceut Sci, Osaka 5691094, Japan Osaka Univ Pharmaceut SciOsaka Japan 5691094 Sci, Osaka 5691094, Japan Kobe Gakuin Univ, Fac Pharmaceut Sci, Nishi Ku, Kobe, Hyogo 65121, Japan Kobe Gakuin Univ Kobe Hyogo Japan 65121 ishi Ku, Kobe, Hyogo 65121, Japan Kobe Gakuin Univ, High Technol Res Ctr, Nishi Ku, Kobe, Hyogo 65121, JapanKobe Gakuin Univ Kobe Hyogo Japan 65121 ishi Ku, Kobe, Hyogo 65121, Japan Kobe Res Projects Thrombosis & Haemostatis, Tarumi Ku, Kobe, Hyogo 6550033, Japan Kobe Res Projects Thrombosis & Haemostatis Kobe Hyogo Japan 6550033 Japan Kobe Univ, Sch Med, Fac Hlth Sci, Suma Ku, Kobe, Hyogo 6540142, Japan KobeUniv Kobe Hyogo Japan 6540142 i, Suma Ku, Kobe, Hyogo 6540142, Japan
Titolo Testata:
JOURNAL OF BIOCHEMISTRY
fascicolo: 3, volume: 129, anno: 2001,
pagine: 455 - 460
SICI:
0021-924X(200103)129:3<455:BDOANL>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
BOVINE TRYPSIN; COMPLEX; RESOLUTION; CRYSTALLOGRAPHY;
Keywords:
binding diversity; crystal structure; noncovalent inhibitor; trypsin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Tomoo, K Osaka Univ Pharmaceut Sci, 4-20-1 Nasahara, Osaka 5691094, Japan Osaka Univ Pharmaceut Sci 4-20-1 Nasahara Osaka Japan 5691094 an
Citazione:
K. Tomoo et al., "Binding diversity of a noncovalent-type low-molecular-weight serine protease inhibitor and function of a catalytic water molecule: X-ray crystal structure of PKSI-527-inhibited trypsin", J BIOCHEM, 129(3), 2001, pp. 455-460

Abstract

PKSI-527 is a noncovalent-type low-molecular-weight inhibitor. The X-ray crystal structure of the trypsin-PKSI-527 complex revealed a binding mode (Form II) different from the previously reported one (Form I) [Nakamura, M. et al. (1995) Biochem. Biophys. Res. Commun. 213, 583-587]. In contrast to the previous case, the electron density of the inhibitor revealed the whole structure clearly. Each structural part of the inhibitor in Forms I and II was differently located at the active site, although the modes of binding of the terminal amino group to the Asp189 carboxyl group were similar. This binding diversity, which is a characteristic of the noncovalent-type low-molecular-weight inhibitor, provides a suitable example for estimating the possible mechanism toward the enzymatic inhibition, together with the structural basis necessary for a specific inhibitor. The mode of binding in Form II reflects the inhibitor-specific situation and is in contrast with the substrate-mimetic binding mode for Form I. Based on the generally accepted catalytic mechanism for serine protease, we propose that a water molecule located at the catalytic site plays an important role in blocking the catalyticfunction of the reactive Ser193 OH group.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/10/20 alle ore 00:30:38