1pk0

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[[Image:1pk0.jpg|left|200px]]
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{{STRUCTURE_1pk0| PDB=1pk0 | SCENE= }}
{{STRUCTURE_1pk0| PDB=1pk0 | SCENE= }}
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'''Crystal Structure of the EF3-CaM complexed with PMEApp'''
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===Crystal Structure of the EF3-CaM complexed with PMEApp===
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==Overview==
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Edema factor (EF), a key virulence factor in anthrax pathogenesis, has calmodulin (CaM)-activated adenylyl cyclase activity. We have found that adefovir dipivoxil, a drug approved to treat chronic infection of hepatitis B virus, effectively inhibits EF-induced cAMP accumulation and changes in cytokine production in mouse primary macrophages. Adefovir diphosphate (PMEApp), the active cellular metabolite of adefovir dipivoxil, inhibits the adenylyl cyclase activity of EF in vitro with high affinity (K(i) = 27 nM). A crystal structure of EF-CaM-PMEApp reveals that the catalytic site of EF forms better van der Waals contacts and more hydrogen bonds with PMEApp than with its endogenous substrate, ATP, providing an explanation for the approximately 10,000-fold higher affinity EF-CaM has for PMEApp versus ATP. Adefovir dipivoxil is a clinically approved drug that can block the action of an anthrax toxin. It can be used to address the role of EF in anthrax pathogenesis.
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The line below this paragraph, {{ABSTRACT_PUBMED_14978283}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 14978283 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14978283}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection., Shen Y, Zhukovskaya NL, Zimmer MI, Soelaiman S, Bergson P, Wang CR, Gibbs CS, Tang WJ, Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):3242-7. Epub 2004 Feb 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14978283 14978283]
Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection., Shen Y, Zhukovskaya NL, Zimmer MI, Soelaiman S, Bergson P, Wang CR, Gibbs CS, Tang WJ, Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):3242-7. Epub 2004 Feb 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14978283 14978283]
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Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins., Shen Y, Lee YS, Soelaiman S, Bergson P, Lu D, Chen A, Beckingham K, Grabarek Z, Mrksich M, Tang WJ, EMBO J. 2002 Dec 16;21(24):6721-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12485993 12485993]
[[Category: Adenylate cyclase]]
[[Category: Adenylate cyclase]]
[[Category: Bacillus anthracis]]
[[Category: Bacillus anthracis]]
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[[Category: Edema factor]]
[[Category: Edema factor]]
[[Category: Prodrug complex]]
[[Category: Prodrug complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:10:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:23:36 2008''

Revision as of 13:23, 27 July 2008

Image:1pk0.png

Template:STRUCTURE 1pk0

Crystal Structure of the EF3-CaM complexed with PMEApp

Template:ABSTRACT PUBMED 14978283

About this Structure

1PK0 is a Protein complex structure of sequences from Bacillus anthracis and Homo sapiens. Full crystallographic information is available from OCA.

Reference

Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection., Shen Y, Zhukovskaya NL, Zimmer MI, Soelaiman S, Bergson P, Wang CR, Gibbs CS, Tang WJ, Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):3242-7. Epub 2004 Feb 20. PMID:14978283

Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins., Shen Y, Lee YS, Soelaiman S, Bergson P, Lu D, Chen A, Beckingham K, Grabarek Z, Mrksich M, Tang WJ, EMBO J. 2002 Dec 16;21(24):6721-32. PMID:12485993

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