4APJ

Human angiotensin-converting enzyme in complex with BPPb

4APJ の概要

• エントリーDOI: 10.2210/pdb4apj/pdb
• 関連するPDBエントリー: 1O86 1O8A 1UZE 1UZF 2C6F 2C6N 2IUL 2IUX 2XY9 2XYD 2YDM 4APH
• 分子名称: ANGIOTENSIN-CONVERTING ENZYME, BRADYKININ-POTENTIATING PEPTIDE B, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: hydrolase-hormone complex, zinc metalloprotease, metallopeptidase, hydrolase/hormone
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71164.67

構造登録者

Masuyer, G.,Schwager, S.L.U.,Sturrock, E.D.,Isaac, R.E.,Acharya, K.R. (登録日: 2012-04-03, 公開日: 2012-10-17, 最終更新日: 2024-11-13)

主引用文献

Masuyer, G.,Schwager, S.L.U.,Sturrock, E.D.,Isaac, R.E.,Acharya, K.R.
Molecular Recognition and Regulation of Human Angiotensin-I Converting Enzyme (Ace) Activity by Natural Inhibitory Peptides.
Sci.Rep., 2:717-, 2012

PubMed 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).

PubMed: 23056909
DOI: 10.1038/SREP00717

実験手法

X-RAY DIFFRACTION (2.6 Å)