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Titolo:
Calcium binding mode of gamma-carboxyglutamic acids in conantokins
Autore:
Lin, CH; Chan, FCH; Hwang, JK; Lyu, PC;
Indirizzi:
Natl Tsing Hua Univ, Dept Life Sci, Hsinchu 30043, Taiwan Natl Tsing Hua Univ Hsinchu Taiwan 30043 Life Sci, Hsinchu 30043, Taiwan
Titolo Testata:
PROTEIN ENGINEERING
fascicolo: 7, volume: 12, anno: 1999,
pagine: 589 - 595
SICI:
0269-2139(199907)12:7<589:CBMOGA>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
METHYL-D-ASPARTATE; NMDA-RECEPTOR ANTAGONIST; SNAIL CONUS-GEOGRAPHUS; VITAMIN-K; PEPTIDES; ION; PROTHROMBIN; SPECTROSCOPY; SIMULATIONS; INHIBITORS;
Keywords:
Cd-113-NMR; calcium binding; gamma-carboxyglutamic acid; circular dichroism; conantokin-T; conantokin-G; free energy perturbation (FEP);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Lyu, PC Natl Tsing Hua Univ, Dept Life Sci, Hsinchu 30043, Taiwan Natl Tsing Hua Univ Hsinchu Taiwan 30043 , Hsinchu 30043, Taiwan
Citazione:
C.H. Lin et al., "Calcium binding mode of gamma-carboxyglutamic acids in conantokins", PROTEIN ENG, 12(7), 1999, pp. 589-595

Abstract

Conantokin-T (con-T) and conantokin-G (Eon-G) are two highly homologous peptide toxins found in Conus venom. The former is a 21-residue peptide with four gamma-carboxyglutammic acid (Gla) residues (at positions 3, 4, 10 and 14), while the latter is a 17-residue peptide with five gamma-carboxyglutamic acid residues (at positions 3, 4, 7, 10 and 14), Despite the apparent similarity in number and relative positions of the gamma-carboxyglutamic acidresidues, Cd-113-NMR studies indicated a distinct metal binding behavior for con-G and con-T. There appears to be four binding sites in con-G in contrast to one metal binding site in con-T. To elucidate the mode of calcium binding by the gamma-carboxyglutamic acid residues in these conantokins, we designed various analogous peptides with their gamma-carboxyglutamic acid replaced by other amino acid residues. Cd-113-NMR experiments on conantokin analogues reveal that the major difference in the number of metal binding sites between con-G and con-T is due to the residue at position 7. We also performed molecular simulations to calculate the relative binding free energies of several potential binding sites. Based on our theoretical and experimental results, we propose a 'four-site' binding model for conantokin-G anda 'single-site' binding model for conantokin-T.

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Documento generato il 02/04/20 alle ore 10:41:43