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Titolo:
THE RELATIVE ORIENTATION OF GLA AND EGF DOMAINS IN COAGULATION-FACTOR-X IS ALTERED BY CA2- A COMBINED NMR SMALL-ANGLE X-RAY-SCATTERING STUDY( BINDING TO THE FIRST EGF DOMAIN )
Autore:
SUNNERHAGEN M; OLAH GA; STENFLO J; FORSEN S; DRAKENBERG T; TREWHELLA J;
Indirizzi:
LUND UNIV,CTR CHEM,POB 124 S-22100 LUND SWEDEN LOS ALAMOS NATL LAB,CHEM SCI & TECHNOL DIV LOS ALAMOS NM 87545 LUND UNIV,MALMO GEN HOSP,WALLENBERG LAB S-21401 MALMO SWEDEN
Titolo Testata:
Biochemistry
fascicolo: 36, volume: 35, anno: 1996,
pagine: 11547 - 11559
SICI:
0006-2960(1996)35:36<11547:TROOGA>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
GAMMA-CARBOXYGLUTAMIC ACID; NUCLEAR-MAGNETIC-RESONANCE; HUMAN FACTOR-IX; PROTEIN STRUCTURAL REQUIREMENTS; CALCIUM-DEPENDENT INTERACTION; BETA-HYDROXYASPARTIC ACID; GROWTH-FACTOR PRECURSOR; FACTOR-LIKE MODULES; MEMBRANE-BINDING; NEUTRON-SCATTERING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
84
Recensione:
Indirizzi per estratti:
Citazione:
M. Sunnerhagen et al., "THE RELATIVE ORIENTATION OF GLA AND EGF DOMAINS IN COAGULATION-FACTOR-X IS ALTERED BY CA2- A COMBINED NMR SMALL-ANGLE X-RAY-SCATTERING STUDY( BINDING TO THE FIRST EGF DOMAIN )", Biochemistry, 35(36), 1996, pp. 11547-11559

Abstract

Coagulation factor X is a serine protease containing three noncatalytic domains: an N-terminal gamma-carboxyglutamic acid (Gla)(1) domain followed by two epidermal growth factor (EGF)-like domains. The isolated N-terminal EGF domain binds Ca2+ with a K-d of 10(-3) M. When linkedto the Gla domain, however, its Ca2+ affinity is increased 10-fold. In this paper, we present the NMR solution structure of the factor X Gla-EGF domain pair with Ca2+ bound to the EGF domain, as well as small angle X-ray scattering (SAXS) data on the Gla-EGF domain pair with andwithout Ca2+. Our results show that Ca2+ binding to the EGF domain makes the cia and EGF domains fold toward each other using the Ca2+ siteas a hinge. Presumably, a similar mechanism may be responsible for alterations in the relative orientation of protein domains in many otherextracellular proteins containing EGF domains with the consensus for Ca2+ binding. The results of the NMR and SAXS measurements reported inthis paper confirm our previous result that the Gla domain is folded also in its apo state when linked to the EGF domain [Sunnerhagen, M., et al. (1995) Nat. Struct. Biol. 2, 504-509]. Finally, our study clearly demonstrates the powerful combination of NMR and SAXS in the study of modular proteins, since this enables reliable evaluation of both short-range (NMR) and long-range interactions (SAXS).

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Documento generato il 26/11/20 alle ore 19:53:51