01799naa a2200253 a 450000100080000000500110000800800410001902400390006010000210009924501240012026000090024452009620025365300360121565300290125165300220128065300150130265300240131765300230134165300160136470000220138070000220140270000160142477301050144010088562020-01-17       2003    bl uuuu     u00u1 u    #d7 a10.1016/S0006-291X(03)01363-92DOI1 aFERNANDEZ, J. H.  aStructural basis of the lisinopril-binding specificity in N- and C-domains of human somatic ACE.h[electronic resource]  c2003  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.  aAngiotensin I-converting enzyme  aBk-potentiating peptides  aHomology modeling  aLisinopril  aModelagem molecular  aMolecular modeling  aSomatic ACE1 aHAYASHI, M. A. F.1 aCAMARGO, A. C. M.1 aNESHICH, G.  tBiochemichal and Biophysical Research Communications, New Yorkgv. 308, n. 2, p. 219-226, Aug. 2003.