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PDBsum entry 4apj

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Hydrolase/hormone PDB id
4apj
Jmol
Contents
Protein chains
581 a.a.
11 a.a.
Ligands
SO4
PE4 ×3
NAG-NAG-BMA
ACT
Metals
_CL ×3
Waters ×124

References listed in PDB file
Key reference
Title Molecular recognition and regulation of human angiotensin-I converting enzyme (ace) activity by natural inhibitory peptides.
Authors G.Masuyer, S.L.Schwager, E.D.Sturrock, R.E.Isaac, K.R.Acharya.
Ref. Sci Rep, 2012, 2, 717. [DOI no: 10.1038/srep00717]
PubMed id 23056909
Abstract
Angiotensin-I converting enzyme (ACE), a two-domain dipeptidylcarboxypeptidase, is a key regulator of blood pressure as a result of its critical role in the renin-angiotensin-aldosterone and kallikrein-kinin systems. Hence it is an important drug target in the treatment of cardiovascular diseases. ACE is primarily known for its ability to cleave angiotensin I (Ang I) to the vasoactive octapeptide angiotensin II (Ang II), but is also able to cleave a number of other substrates including the vasodilator bradykinin and N-acetyl-Ser-Asp-Lys-Pro (Ac-SDKP), a physiological modulator of hematopoiesis. For the first time we provide a detailed biochemical and structural basis for the domain selectivity of the natural peptide inhibitors of ACE, bradykinin potentiating peptide b and Ang II. Moreover, Ang II showed selective competitive inhibition of the carboxy-terminal domain of human somatic ACE providing evidence for a regulatory role in the human renin-angiotensin system (RAS).
PROCHECK
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 Headers