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8QHL

Human Angiotensin-1 converting enzyme N-domain in complex with the lactotripeptide VPP

Summary for 8QHL
Entry DOI10.2210/pdb8qhl/pdb
DescriptorAngiotensin-converting enzyme, 1,2-ETHANEDIOL, TETRAETHYLENE GLYCOL, ... (16 entities in total)
Functional Keywordsangiotensin-i converting enzyme, zinc-dependent endopeptidase, di-peptidyl carboxxypeptidase, hydrolase
Biological sourceHomo sapiens (human)
More
Total number of polymer chains4
Total formula weight150677.42
Authors
Gregory, K.S.,Cozier, G.E.,Acharya, K.R. (deposition date: 2023-09-08, release date: 2023-11-22, Last modification date: 2024-10-09)
Primary citationGregory, K.S.,Cozier, G.E.,Schwager, S.L.U.,Sturrock, E.D.,Acharya, K.R.
Structural insights into the inhibitory mechanism of angiotensin-I-converting enzyme by the lactotripeptides IPP and VPP.
Febs Lett., 598:242-251, 2024
Cited by
PubMed Abstract: Human somatic angiotensin-1-converting enzyme (sACE) is composed of a catalytic N-(nACE) and C-domain (cACE) of similar size with different substrate specificities. It is involved in the regulation of blood pressure by converting angiotensin I to the vasoconstrictor angiotensin II and has been a major focus in the development of therapeutics for hypertension. Bioactive peptides from various sources, including milk, have been identified as natural ACE inhibitors. We report the structural basis for the role of two lacototripeptides, Val-Pro-Pro and Ile-Pro-Pro, in domain-specific inhibition of ACE using X-ray crystallography and kinetic analysis. The lactotripeptides have preference for nACE due to altered polar interactions distal to the catalytic zinc ion. Elucidating the mechanism of binding and domain selectivity of these peptides also provides important insights into the functional roles of ACE.
PubMed: 37904282
DOI: 10.1002/1873-3468.14768
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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