Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
THE NA+ BINDING-SITE OF THROMBIN
Autore:
DICERA E; GUINTO ER; VINDIGNI A; DANG QD; AYALA YM; WUYI M; TULINSKY A;
Indirizzi:
WASHINGTON UNIV,SCH MED,DEPT BIOCHEM & MOLEC BIOPHYS,BOX 8231 ST LOUIS MO 63110 MICHIGAN STATE UNIV,DEPT CHEM E LANSING MI 48824
Titolo Testata:
The Journal of biological chemistry
fascicolo: 38, volume: 270, anno: 1995,
pagine: 22089 - 22092
SICI:
0021-9258(1995)270:38<22089:TNBOT>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN ALPHA-THROMBIN; PRO-ARG CHLOROMETHYLKETONE; CRYSTAL-STRUCTURE; ACTIVATED ENZYME; TRP INSERTION; PROTEIN-C; SPECIFICITY; COMPLEXES; CATIONS;
Tipo documento:
Note
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
E. Dicera et al., "THE NA+ BINDING-SITE OF THROMBIN", The Journal of biological chemistry, 270(38), 1995, pp. 22089-22092

Abstract

Thrombin is an allosteric serine protease existing in two forms, slowand fast, targeted toward anticoagulant and procoagulant activities, The slow --> fast transition is induced by Na+ binding to a site contained within a cylindrical cavity formed by three antiparallel beta-strands of the B-chain (Met(180)-Tyr(184a), Lys(224)-Tyr(228), and Val(213)-Gly(219)) diagonally crossed by the Glu(188) Glu(192) strand, The site is shaped further by the loop connecting the last two beta-strandsand is located more than 15 Angstrom away from the catalytic triad. The cavity traverses through thrombin from the active site to the opposite surface and contains Asp(189) of the primary specificity site nearits midpoint, The bound Na+ is coordinated octahedrally by the carbonyl oxygen atoms of Tyr(184a), Arg(221a), and Lys(224), and by three highly conserved water molecules in the D-Phe-Pro-Arg chloromethylketonethrombin. The sequence in the Na+ binding loop is highly conserved inthrombin from II different species and is homologous to that found inother serine proteases involved in blood coagulation, Mutation of twoAsp residues flanking Arg(221a) (D221A/D222K) almost abolishes the allosteric properties of thrombin and shows that the Na+ binding loop isalso involved in direct recognition of protein C and antithrombin.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/07/20 alle ore 22:33:39