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Titolo:
LG/LNS domains: multiple functions - one business end?
Autore:
Rudenko, G; Hohenester, E; Muller, YA;
Indirizzi:
Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 ward Hughes Med Inst, Dallas, TX 75390 USA 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 Imperial Coll, Blackett Lab, Biophys Sect, London SW7 2AZ, England Imperial Coll London England SW7 2AZ ophys Sect, London SW7 2AZ, England Imperial Coll, Div Med, London SW7 2AZ, England Imperial Coll London England SW7 2AZ l, Div Med, London SW7 2AZ, England Max Delbruck Ctr Mol Med, Forschungsgrp Kristallog, D-13092 Berlin, Germany Max Delbruck Ctr Mol Med Berlin Germany D-13092 D-13092 Berlin, Germany
Titolo Testata:
TRENDS IN BIOCHEMICAL SCIENCES
fascicolo: 6, volume: 26, anno: 2001,
pagine: 363 - 368
SICI:
0968-0004(200106)26:6<363:LDMF-O>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
LAMININ G-LIKE; HORMONE-BINDING GLOBULIN; ALPHA-DYSTROGLYCAN BINDING; CARBOHYDRATE-RECOGNITION; CRYSTAL-STRUCTURE; CELL-SURFACE; PROTEIN-S; HEPARIN; RECEPTOR; AGRIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Rudenko, G Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 Med Inst, Dallas, TX 75390 USA
Citazione:
G. Rudenko et al., "LG/LNS domains: multiple functions - one business end?", TRENDS BIOC, 26(6), 2001, pp. 363-368

Abstract

The three-dimensional structures of LG/LNS domains from neurexin, the laminin alpha2 chain and sex hormone-binding globulin reveal a close structuralrelationship to the carbohydrate-binding pentraxins and other lectins, However, these LG/LNS domains appear to have a preferential ligand-interactionsite distinct from the carbohydrate-binding sites found in lectins, and this interaction site accommodates not only sugars but also steroids and proteins. In fact, the LG/LNS domain interaction site has features reminiscent of the antigen-combining sites in immunoglobulins. The LG/LNS domain presents an interesting case in which the fold has remained conserved but the functional sites have evolved; consequently, making predictions of structure-function relationships on the basis of the lectin fold alone is difficult.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 11:33:18