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Titolo:
CALCIUM-BINDING TO TANDEM REPEATS OF EGF-LIKE MODULES - EXPRESSION AND CHARACTERIZATION OF THE EGF-LIKE MODULES OF HUMAN NOTCH-1 IMPLICATEDIN RECEPTOR-LIGAND INTERACTIONS
Autore:
RAND MD; LINDBLOM A; CARLSON J; VILLOUTREIX BO; STENFLO J;
Indirizzi:
LUND UNIV,UNIV HOSP,DEPT CLIN CHEM S-20502 MALMO SWEDEN LUND UNIV,UNIV HOSP,DEPT CLIN CHEM S-20502 MALMO SWEDEN
Titolo Testata:
Protein science
fascicolo: 10, volume: 6, anno: 1997,
pagine: 2059 - 2071
SICI:
0961-8368(1997)6:10<2059:CTTROE>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPIDERMAL GROWTH-FACTOR; FACTOR-LIKE DOMAINS; FACTOR-X; FACTOR-IX; NUCLEOTIDE-SEQUENCE; HUMAN FIBRILLIN-1; DROSOPHILA NOTCH; HUMAN HOMOLOG; PROTEIN; GENE;
Keywords:
CA2+-BINDING; EGF-LIKE MODULES; NOTCH; DELTA; SERRATE; RECEPTOR-LIGAND INTERACTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
49
Recensione:
Indirizzi per estratti:
Citazione:
M.D. Rand et al., "CALCIUM-BINDING TO TANDEM REPEATS OF EGF-LIKE MODULES - EXPRESSION AND CHARACTERIZATION OF THE EGF-LIKE MODULES OF HUMAN NOTCH-1 IMPLICATEDIN RECEPTOR-LIGAND INTERACTIONS", Protein science, 6(10), 1997, pp. 2059-2071

Abstract

The Ca2+-binding epidermal growth factor (cbECF)-like module is a structural component of numerous diverse proteins and occurs almost exclusively within repeated motifs. Notch-1, a fundamental receptor for cell fate decisions, contains 36 extracellular EGF modules in tandem, of which 21 are potentially Ca2+ binding. We report the Ca2+-binding properties of EGF11-12 and EGF10-13 from human Notch-1 (hNEGF11-12 and hNEGF10-13), modules previously shown to support Ca2+-dependent interactions with the ligands Delta and Serrate. Ca2+ titrations in the presence of chromophoric chelators, 5,5'-Br(2)BAPTA and 5-NBAPTA, gave two binding constants for hNEGF11-12, K-dl=3.4 X 10(-5) M and K-d2 > 2.5 X 10(-4) M. The high-affinity site was found to be localized to hNEGF12. Titration of hNEGF10-13 gave three binding constants, K-dl=3.1 X 10(-6) M, K-d2=1.6 X 10(-4) M, and K-d3 > 2.5 X 10(-4) M, demonstrating that assembly of EGF modules in tandem can increase Ca2+ affinity. The highest affinity sites in hNEGF11-12 and hNEGF10-13 had 10 to 100-fold higher affinity than reported for EGF32-33 and EGF25-31, respectively, from fibrillin-1, a connective tissue protein with 43 cbEGF modules. Amodel of hNEGF11-12 based on fibrillin-1 EGF32-33 demonstrates electronegative potential that could contribute to the higher affinity of the Ca2+-binding site in hNEGF12. These data demonstrate that the Ca2+ affinity of cbEGF repeats can be highly variable among different classes of cbEGF containing proteins.

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Documento generato il 30/05/20 alle ore 15:13:59