Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
AN EXTRACELLULAR BETA-PROPELLER MODULE PREDICTED IN LIPOPROTEIN AND SCAVENGER RECEPTORS, TYROSINE KINASES, EPIDERMAL GROWTH-FACTOR PRECURSOR, AND EXTRACELLULAR-MATRIX COMPONENTS
Autore:
SPRINGER TA;
Indirizzi:
CTR BLOOD RES,200 LONGWOOD AVE BOSTON MA 02115 HARVARD UNIV,SCH MED,DEPT PATHOL BOSTON MA 02115
Titolo Testata:
Journal of Molecular Biology
fascicolo: 4, volume: 283, anno: 1998,
pagine: 837 - 862
SICI:
0022-2836(1998)283:4<837:AEBMPI>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
LDL-RECEPTOR; CRYSTAL-STRUCTURE; FAMILIAL HYPERCHOLESTEROLEMIA; PROTEIN FOLD; DROSOPHILA-MELANOGASTER; MUTATIONAL ANALYSIS; EGF PRECURSOR; 2.0 ANGSTROM; GENE; BINDING;
Keywords:
STRUCTURE PREDICTION; BETA-PROPELLER; LOW DENSITY LIPOPROTEIN RECEPTOR; EPIDERMAL GROWTH FACTOR PRECURSOR; NIDOGEN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
83
Recensione:
Indirizzi per estratti:
Citazione:
T.A. Springer, "AN EXTRACELLULAR BETA-PROPELLER MODULE PREDICTED IN LIPOPROTEIN AND SCAVENGER RECEPTORS, TYROSINE KINASES, EPIDERMAL GROWTH-FACTOR PRECURSOR, AND EXTRACELLULAR-MATRIX COMPONENTS", Journal of Molecular Biology, 283(4), 1998, pp. 837-862

Abstract

An abundant, widely dispersed, extracellular sequence repeat that contains a consensus YWTD motif is shown here to occur in groups of six contiguous repeats. Thirteen lines of evidence, including experimental and computational data, predict with p < 3 x 10(-9) that the repeats do not form tandem domains, but rather each group of six repeats folds into a compact beta-propeller structure. The six beta-sheets are arranged about a 6-fold pseudosymmetry axis, and each repeat contributes loops to the faces surrounding the pseudosymmetry axis. Seven different endocytic receptors that contain from one to eight YWTD beta-propellerdomains act as lipoprotein, vitellogenin, and scavenger receptors. Inthe low density lipoprotein receptor (LDLR), the many mutations in familial hypercholesterolaemia that map to the YWTD domain can now be interpreted. In the extracellular matrix component nidogen, the YWTD domain functions to bind laminin. Three YWTD domains and interspersed fibronectin type III (FN3) domains constitute almost the entire extracellular domain of the sevenless and c-ros receptor tyrosine kinases. YWTDdomains often are bounded by epidermal growth factor (EGF) modules, including in the EGF precursor itself. YWTD beta-propellers have a circular folding pattern that brings neighboring modules into close proximity, and may have important consequences for the architecture of multi-domain proteins. (C) 1998 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:54:57