Angiotensin-Converting Enzyme: Difference between revisions
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During the SARS scare of 2002-2003, extensive research was focused on the interactions between the SARS virus and its host cells. It was determined that the severe acute respiratory syndrome conavirus (SARS-CoV) enters cells through the activities of a spike shaped protein on its outer envelope. <ref name="SARS">PMID:18448527</ref> The Receptor Binding Domain (RBD) of SARS-CoV binds to ACE2, on the surface of the cell. It was determined that by changing a few selected residues on either the SARS-CoV RBD or the ACE2 binding site, the virus becomes significantly more infectious. <scene name='Angiotensin-Converting_Enzyme/Sars/2'>It is believed that these mutations</scene> ([[3d0g]]), namely at residues 31, 35, 38, & 353 in ACE2 or residues 479 and 487 in the SARS-CoV RBD, are what allowed for SARS transmission from [http://en.wikipedia.org/wiki/Civet Civets] to Humans. In fact, in those SARS strains which were determined to be most infectious, the unfavorable electrostatic interactions at the binding interface were removed via mutations at the critical residues 479 and 487. <ref name="SARS"/> | During the SARS scare of 2002-2003, extensive research was focused on the interactions between the SARS virus and its host cells. It was determined that the severe acute respiratory syndrome conavirus (SARS-CoV) enters cells through the activities of a spike shaped protein on its outer envelope. <ref name="SARS">PMID:18448527</ref> The Receptor Binding Domain (RBD) of SARS-CoV binds to ACE2, on the surface of the cell. It was determined that by changing a few selected residues on either the SARS-CoV RBD or the ACE2 binding site, the virus becomes significantly more infectious. <scene name='Angiotensin-Converting_Enzyme/Sars/2'>It is believed that these mutations</scene> ([[3d0g]]), namely at residues 31, 35, 38, & 353 in ACE2 or residues 479 and 487 in the SARS-CoV RBD, are what allowed for SARS transmission from [http://en.wikipedia.org/wiki/Civet Civets] to Humans. In fact, in those SARS strains which were determined to be most infectious, the unfavorable electrostatic interactions at the binding interface were removed via mutations at the critical residues 479 and 487. <ref name="SARS"/> | ||
</StructureSection> | </StructureSection> | ||
== | ==3D Structures of Angiotensin-Converting Enzyme== | ||
[[1o8a]] – hANCE - human<br /> | [[1o8a]] – hANCE - human<br /> | ||