2a5k: Difference between revisions

Revision as of 20:17, 28 July 2008

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File:2a5k.png

Template:STRUCTURE 2a5k

Crystal structures of SARS coronavirus main peptidase inhibited by an aza-peptide epoxide in space group P212121Crystal structures of SARS coronavirus main peptidase inhibited by an aza-peptide epoxide in space group P212121

Template:ABSTRACT PUBMED 16219322

About this StructureAbout this Structure

2A5K is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide., Lee TW, Cherney MM, Huitema C, Liu J, James KE, Powers JC, Eltis LD, James MN, J Mol Biol. 2005 Nov 11;353(5):1137-51. Epub 2005 Sep 27. PMID:16219322

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structures of SARS coronavirus main peptidase inhibited by an aza-peptide epoxide in space group P212121'''
+===Crystal structures of SARS coronavirus main peptidase inhibited by an aza-peptide epoxide in space group P212121===
-==Overview==
+<!--
-The main peptidase (M(pro)) from the coronavirus (CoV) causing severe acute respiratory syndrome (SARS) is one of the most attractive molecular targets for the development of anti-SARS agents. We report the irreversible inhibition of SARS-CoV M(pro) by an aza-peptide epoxide (APE; k(inact)/K(i) = 1900(+/-400) M(-1) s(-1)). The crystal structures of the M(pro):APE complex in the space groups C2 and P2(1)2(1)2(1) revealed the formation of a covalent bond between the catalytic Cys145 S(gamma) atom of the peptidase and the epoxide C3 atom of the inhibitor, substantiating the mode of action of this class of cysteine-peptidase inhibitors. The aza-peptide component of APE binds in the substrate-binding regions of M(pro) in a substrate-like manner, with excellent structural and chemical complementarity. In addition, the crystal structure of unbound M(pro) in the space group C2 revealed that the "N-fingers" (N-terminal residues 1 to 7) of both protomers of M(pro) are well defined and the substrate-binding regions of both protomers are in the catalytically competent conformation at the crystallization pH of 6.5, contrary to the previously determined crystal structures of unbound M(pro) in the space group P2(1).
+The line below this paragraph, {{ABSTRACT_PUBMED_16219322}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16219322 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16219322}}
 ==About this Structure==
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 [[Category: Specificity pocket]]
 [[Category: Substrate-like inhibitor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:38:05 2008''
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