Data/hora: 04/06/2024 02:13:02

Biblioteca(s): 	Embrapa Agricultura Digital.	
Data corrente: 	15/04/2004	
Data da última atualização: 	17/01/2020	
Autoria: 	FERNANDEZ, J. H.; HAYASHI, M. A. F.; CAMARGO, A. C. M.; NESHICH, G.	
Afiliação: 	JORGE H. FERNANDEZ, Instituto Butantan; MIRIAN A. F. HAYASHI, Instituto Butantan; ANTONIO C. M. CAMARGO, Instituto Butantan; GORAN NESHICH, CNPTIA.	
Título: 	Structural basis of the lisinopril-binding specificity in N- and C-domains of human somatic ACE.	
Ano de publicação: 	2003	
Fonte/Imprenta: 	Biochemichal and Biophysical Research Communications, New York, v. 308, n. 2, p. 219-226, Aug. 2003.	
DOI: 	10.1016/S0006-291X(03)01363-9	
Idioma: 	Inglês	
Conteúdo: 	Angiotensin I-converting enzyme (ACE) is a dipeptidylcarboxypeptidase which converts angiotensin I into the vasopressor peptide angiotensin II and also inactivates the hypotensive peptide bradykinin, playing an important role in blood pressure regulation. The present work describes the molecular modeling of the N-terminal human somatic ACE in complex with the inhibitor lisinopril, identifying the residues involved in the inhibitor-binding pocket. The obtained results identify differences in the lisinopril lysine moiety-binding residues for N- and C-terminals of sACE domains and an important carboxy-terminal proline hydrophobic accommodations mediated by the aromatic ring of Tyr532 and Tyr1128 residues, respectively. The present model will be useful for the development of a new inhibitor family based on the natural BPP peptides and derivatives, or even to improve the binding capacities and the domain specificity of the already known inhibitors.	
Palavras-Chave: 	Angiotensin I-converting enzyme; Bk-potentiating peptides; Homology modeling; Lisinopril; Modelagem molecular; Molecular modeling; Somatic ACE.	
Categoria do assunto: 	X Pesquisa, Tecnologia e Engenharia	
Registro original: 	Embrapa Agricultura Digital (CNPTIA)	
Exemplares: 	CNPTIA - (10213-1) - UPC - AP - -- -  -  - 2004.00004 - DES
CNPTIA - (10213-2) - UPC - AP - DD -  -  -  - DIS