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Titolo:
Localization of formylpeptide binding domain using chimeric and mutagenesis approaches
Autore:
Zhu, JQ; Lu, J; Shi, XQ; Zhang, MY; Zhu, DX;
Indirizzi:
Nanjing Univ, Dept Biochem, State Key Lab Pharmaceut Biotechnol, Nanjing 210093, Peoples R China Nanjing Univ Nanjing Peoples R China 210093 jing 210093, Peoples R China
Titolo Testata:
PROGRESS IN NATURAL SCIENCE
fascicolo: 7, volume: 9, anno: 1999,
pagine: 524 - 531
SICI:
1002-0071(199907)9:7<524:LOFBDU>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
FORMYL PEPTIDE RECEPTOR; LEUKOCYTE CHEMOATTRACTANT RECEPTORS; ANAPHYLATOXIN; SPECIFICITY; CDNA;
Keywords:
N-formylpeptide receptors; FMLP; chimeric receptor; chemotactic factors;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
16
Recensione:
Indirizzi per estratti:
Indirizzo: Zhu, DX Nanjing Univ, Dept Biochem, State Key Lab Pharmaceut Biotechnol, Nanjing 210093, Peoples R China Nanjing Univ Nanjing Peoples R China 210093 093, Peoples R China
Citazione:
J.Q. Zhu et al., "Localization of formylpeptide binding domain using chimeric and mutagenesis approaches", PROG NAT SC, 9(7), 1999, pp. 524-531

Abstract

The N-formylpeptide fMet-Leu-Phe (fMLP) is a small chemotactic peptide derived from bacterial proteins and it is a potent activator for neutrophil functions. Understanding of its binding to the fMLP receptor (FPR) is inflammation chimeric and point mutant FPR, the following results were obtained: (i) The amino terminal domain of the FPR is a less important region for fMLPbinding, as compared to other receptors such as the C5a receptor and the IL-8 receptors;. (ii) All three extracellular loops are involved in fMLP binding, but the first and third loops are more important than the second loop. (iii) Several point mutations in the transmembrane domains (TMD) disrupted fMLP binding, indicating amino acid residues in the TMDs also participated in fMLP binding. These results are helpful in designing new antagonists for the FPR.

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Documento generato il 23/01/21 alle ore 09:11:44