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Titolo:
Three-dimensional model of the SHBG-like region of anticoagulant protein S: New structure-function insights
Autore:
Villoutreix, BO; Dahlback, B; Borgel, D; Gandrille, S; Muller, YA;
Indirizzi:
Univ Paris 05, Sch Pharm, INSERM, U428, F-75006 Paris, France Univ Paris 05 Paris France F-75006 , INSERM, U428, F-75006 Paris, France Univ Lund, Wallenberg Lab, Malmo, Sweden Univ Lund Malmo SwedenUniv Lund, Wallenberg Lab, Malmo, Sweden Max Delbruck Ctr Mol Med, Forschungsgrp Kristallog, Berlin, Germany Max Delbruck Ctr Mol Med Berlin Germany grp Kristallog, Berlin, Germany
Titolo Testata:
PROTEINS-STRUCTURE FUNCTION AND GENETICS
fascicolo: 2, volume: 43, anno: 2001,
pagine: 203 - 216
SICI:
0887-3585(20010501)43:2<203:TMOTSR>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
LAMININ G-LIKE; NATURALLY-OCCURRING MUTATIONS; HUMAN C4B-BINDING PROTEIN; ANDROGEN-BINDING PROTEIN; DEFICIENCY TYPE-I; G-LIKE DOMAIN; POINT MUTATIONS; MOLECULAR-BASIS; FACTOR VA; ALPHA-DYSTROGLYCAN;
Keywords:
protein modeling; blood coagulation; thrombosis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
86
Recensione:
Indirizzi per estratti:
Indirizzo: Villoutreix, BO Univ Paris 05, Sch Pharm, INSERM, U428, 4 Ave Observ, F-75006 Paris, France Univ Paris 05 4 Ave Observ Paris France F-75006 s, France
Citazione:
B.O. Villoutreix et al., "Three-dimensional model of the SHBG-like region of anticoagulant protein S: New structure-function insights", PROTEINS, 43(2), 2001, pp. 203-216

Abstract

Protein S (PS) is a vitamin K-dependent glycoprotein that consists of several modules including a C-terminal sex hormone-binding globulin (SHBG)-likedomain that has been subdivided into two laminin LG-type domains, The SHBG-like region of PS is known to bind to a complement regulator molecule, C4b-binding protein (C4BP), coagulation factor Va (FVa) and receptor tyrosine kinases. Inherited PS deficiency has been associated with thromboembolic disease, Yet, study of the mechanisms by which the SI-IBG-like region of PS serves its essential functions has so far been hampered because of the lack of structural information. Recently, the three-dimensional (3D) structure of LG domains from plasma SHBG, laminin and neurexin have been reported and were found related to the pentraxin family, We used these X-ray structures to build homology models of the SHBG like region of human PS, We then analyzed previously reported experimental/clinical data in the light of the predicted structures. A potential calcium-binding site is found in the first LGdomain of PS and D292 could play a role in this process, This region is close to the interface between the two LG domains and is also surrounded by segments that have been suggested by synthetic peptide studies to be important for C4BP or FVa binding. The 39 point mutations linked to PS deficiencies or reported as neutral variants were rationalized in the 3D structure. (C) 2001 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 11:48:00