ACE2/structural biology project: Difference between revisions

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Human ACE2 enzyme is composed of 805 amino acids.
Human ACE2 enzyme is composed of 805 amino acids.
Extracelular region of the human ACE2 enzyme is composed of an N-terminal zinc metallopeptidase domain and a C-terminal collectrin-like domain ended with a transmembrane helix.
Extracelular region of the human ACE2 enzyme is composed of an N-terminal zinc metallopeptidase domain and a C-terminal collectrin-like domain ended with a transmembrane helix.
Subdomains I(N-terminus) and II(C-terminus) of the metallopeptidase domain of ACE2 form two sides of a cleft and connected at the floor of the active site of the cleft. Helix 17 (residues 511-531) connects to the subdomains and forms part of the floor.
The secondary structure of the metallopeptidase domain of the ACE2 is composed of 20 alpha-helical segments and 9 more helical segments. Only 6 short betta-structural segments are present<ref>PMID: 14754895</ref>.
Near the bottom and subdomain I sidethere is a location of the zinc-binding site. Zinc is coordinate by His374, His378, Glu402 and a water molecule <ref>PMID: 14754895</ref>.
A chloride ion is coordinated by Arg169, Trp477, and Lys481 in subdomain II.
== ACE2-B0AT1 complex ==
In the context of the complex, dimerisation of the ACE2 is mediated by neck domain. That complex has both open and closed conformations observed<ref>PMID: 14754895</ref>. 




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ACE2 gene is located in Chromosome X on forward strand.  
ACE2 gene is located in Chromosome X on forward strand.  


== Desease ==
Cardiovascular disease is associated with activation of the signaling pathways. ACE2 is localized in various tissues of the cardiovascular system <ref>PMID: 24332999 </ref>. Underexpression of the ACE2 results neutrophic inflamation in the infarct and pre-infarct regions<ref>PMID: 19808375 </ref>.


Also ACE2 plays role in regulation of the blood pressure<ref>PMID: 16788004</ref>. Highly expressed enzyme protects against hypertension.
== References ==
== References ==
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