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Registro Completo |
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
15/04/2004 |
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Data da última atualização: |
17/01/2020 |
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Autoria: |
FERNANDEZ, J. H.; HAYASHI, M. A. F.; CAMARGO, A. C. M.; NESHICH, G. |
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Afiliação: |
JORGE H. FERNANDEZ, Instituto Butantan; MIRIAN A. F. HAYASHI, Instituto Butantan; ANTONIO C. M. CAMARGO, Instituto Butantan; GORAN NESHICH, CNPTIA. |
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Título: |
Structural basis of the lisinopril-binding specificity in N- and C-domains of human somatic ACE. |
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Ano de publicação: |
2003 |
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Fonte/Imprenta: |
Biochemichal and Biophysical Research Communications, New York, v. 308, n. 2, p. 219-226, Aug. 2003. |
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DOI: |
10.1016/S0006-291X(03)01363-9 |
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Idioma: |
Inglês |
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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. |
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Palavras-Chave: |
Angiotensin I-converting enzyme; Bk-potentiating peptides; Homology modeling; Lisinopril; Modelagem molecular; Molecular modeling; Somatic ACE. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
LEADER 01799naa a2200253 a 4500
001 1008856
005 2020-01-17
008 2003 bl uuuu u00u1 u #d
024 7 $a10.1016/S0006-291X(03)01363-9$2DOI
100 1 $aFERNANDEZ, J. H.
245 $aStructural basis of the lisinopril-binding specificity in N- and C-domains of human somatic ACE.$h[electronic resource]
260 $c2003
520 $aAngiotensin 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.
653 $aAngiotensin I-converting enzyme
653 $aBk-potentiating peptides
653 $aHomology modeling
653 $aLisinopril
653 $aModelagem molecular
653 $aMolecular modeling
653 $aSomatic ACE
700 1 $aHAYASHI, M. A. F.
700 1 $aCAMARGO, A. C. M.
700 1 $aNESHICH, G.
773 $tBiochemichal and Biophysical Research Communications, New York$gv. 308, n. 2, p. 219-226, Aug. 2003.
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