Crystal Structure of the N Domain of Human Somatic Angiotensin I-converting Enzyme Provides a Structural Basis for Domain-specific Inhibitor Design

2006 ◽  
Vol 357 (3) ◽  
pp. 964-974 ◽  
Author(s):  
Hazel R. Corradi ◽  
Sylva L.U. Schwager ◽  
Aloysius T. Nchinda ◽  
Edward D. Sturrock ◽  
K. Ravi Acharya
Keyword(s):  
Crystal Structure ◽  
Specific Inhibitor ◽  
Structural Basis ◽  
Converting Enzyme ◽  
Inhibitor Design ◽  
Angiotensin I ◽  
Domain Specific ◽  
Angiotensin I Converting Enzyme

scholarly journals Structural basis of Ac-SDKP hydrolysis by Angiotensin-I converting enzyme

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Geoffrey Masuyer ◽  
Ross G. Douglas ◽  
Edward D. Sturrock ◽  
K. Ravi Acharya
Keyword(s):  
Structural Basis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme

The high-resolution crystal structure of phosphatidylinositol 4-kinase IIβ and the crystal structure of phosphatidylinositol 4-kinase IIα containing a nucleoside analogue provide a structural basis for isoform-specific inhibitor design

2015 ◽  
Vol 71 (7) ◽  
pp. 1555-1563 ◽  
Author(s):  
Martin Klima ◽  
Adriana Baumlova ◽  
Dominika Chalupska ◽  
Hubert Hřebabecký ◽  
Milan Dejmek ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Nucleoside Analogue ◽  
Specific Inhibitor ◽  
Eukaryotic Cells ◽  
Structural Basis ◽  
Conformational Heterogeneity ◽  
Inhibitor Design ◽  
Hydrophobic Pocket ◽  
Phosphatidylinositol 4

Phosphatidylinositol 4-phosphate (PI4P) is the most abundant monophosphoinositide in eukaryotic cells. Humans have four phosphatidylinositol 4-kinases (PI4Ks) that synthesize PI4P, among which are PI4K IIβ and PI4K IIα. In this study, two crystal structures are presented: the structure of human PI4K IIβ and the structure of PI4K IIα containing a nucleoside analogue. The former, a complex with ATP, is the first high-resolution (1.9 Å) structure of a PI4K. These structures reveal new details such as high conformational heterogeneity of the lateral hydrophobic pocket of the C-lobe and together provide a structural basis for isoform-specific inhibitor design.

No Association of Angiotensin I Converting Enzyme I/D Polymorphism with Domain-Specific Cognitive Function in Aged Men without Dementia

2011 ◽  
Vol 13 (3) ◽  
pp. 212-216 ◽  
Author(s):  
Mu-En Liu ◽  
Shih-Jen Tsai ◽  
Ti Lu ◽  
Cheng-Jee Hong ◽  
Ming-Chao Chen ◽  
...  
Keyword(s):  
Cognitive Function ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Domain Specific ◽  
Angiotensin I Converting Enzyme ◽  
Enzyme I

Angiotensin-I converting enzyme (ACE): structure, biological roles, and molecular basis for chloride ion dependence

2014 ◽  
Vol 395 (10) ◽  
pp. 1135-1149 ◽  
Author(s):  
Geoffrey Masuyer ◽  
Christopher J. Yates ◽  
Edward D. Sturrock ◽  
K. Ravi Acharya
Keyword(s):  
Molecular Mechanisms ◽  
Chloride Ion ◽  
Chloride Ions ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
X Ray Crystallography ◽  
Domain Specific ◽  
Angiotensin I Converting Enzyme ◽  
Zinc Protease

Abstract Somatic angiotensin-I converting enzyme (sACE) has an essential role in the regulation of blood pressure and electrolyte fluid homeostasis. It is a zinc protease that cleaves angiotensin-I (AngI), bradykinin, and a broad range of other signalling peptides. The enzyme activity is provided by two homologous domains (N- and C-), which display clear differences in substrate specificities and chloride activation. The presence of chloride ions in sACE and its unusual role in activity was identified early on in the characterisation of the enzyme. The molecular mechanisms of chloride activation have been investigated thoroughly through mutagenesis studies and shown to be substrate-dependent. Recent results from X-ray crystallography structural analysis have provided the basis for the intricate interactions between ACE, its substrate and chloride ions. Here we describe the role of chloride ions in human ACE and its physiological consequences. Insights into the chloride activation of the N- and C-domains could impact the design of improved domain-specific ACE inhibitors.

Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril 1

FEBS Letters ◽  
2003 ◽  
Vol 538 (1-3) ◽  
pp. 65-70 ◽  
Author(s):  
Ho Min Kim ◽  
Dong Ryeol Shin ◽  
Ook Joon Yoo ◽  
Hayyoung Lee ◽  
Jie-Oh Lee
Keyword(s):  
Crystal Structure ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme

Relationships between angiotensin I converting enzyme gene polymorphism, plasma levels, and diabetic retinal and renal complications

Diabetes ◽  
1994 ◽  
Vol 43 (3) ◽  
pp. 384-388 ◽  
Author(s):  
M. Marre ◽  
P. Bernadet ◽  
Y. Gallois ◽  
F. Savagner ◽  
T. T. Guyene ◽  
...  
Keyword(s):  
Gene Polymorphism ◽  
Plasma Levels ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Enzyme Gene ◽  
Angiotensin I Converting Enzyme ◽  
Renal Complications

Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Elk (Cervus elaphus) Velvet Antler

2005 ◽  
Vol 10 (3) ◽  
pp. 239-243 ◽  
Author(s):  
Rohan Karawita ◽  
Pyo-Jam park ◽  
Nalin Siriwardhana ◽  
Byong-Tae Jeon ◽  
Sang-Ho Moon ◽  
...  
Keyword(s):  
Cervus Elaphus ◽  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Velvet Antler ◽  
Ace Inhibitory
Sign in / Sign up

Export Citation Format

Share Document