2fun

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[[Image:2fun.gif|left|200px]]
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{{Seed}}
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[[Image:2fun.png|left|200px]]
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{{STRUCTURE_2fun| PDB=2fun | SCENE= }}
{{STRUCTURE_2fun| PDB=2fun | SCENE= }}
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'''alternative p35-caspase-8 complex'''
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===alternative p35-caspase-8 complex===
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==Overview==
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Wide-spectrum caspase inhibition by the baculoviral p35 protein was previously shown to be a consequence of covalent inhibition in which a thioester bond is stably formed between the cleavage residue Asp87 of p35 and the active site Cys360' of caspase-8. Here we show that the N-terminal fragment of cleaved p35 (p35-N) is a circular peptide when dissociated from the caspase. Biochemical and crystallographic data suggest that p35-N circularization results from the trapping of a native chemical ligation intermediate in the p35/caspase complex, in which the N-terminal Cys2 of p35 attacks the Asp87-Cys360' thioester to form an equilibrium between Asp87-Cys2 and Asp87-Cys360'. This provides a crucial covalent interaction for keeping the N terminus of p35 bound in the caspase active site, which explains the absolute requirement of Cys2 for caspase inhibition. Participation of native chemical ligation in caspase inhibition by p35 illustrates an unusual mechanism of protease inhibition.
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The line below this paragraph, {{ABSTRACT_PUBMED_16492559}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16492559 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16492559}}
==About this Structure==
==About this Structure==
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[[Category: Wu, H.]]
[[Category: Wu, H.]]
[[Category: Apoptosis/hydrolase]]
[[Category: Apoptosis/hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:19:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:25:39 2008''

Revision as of 10:25, 27 July 2008

Image:2fun.png

Template:STRUCTURE 2fun

alternative p35-caspase-8 complex

Template:ABSTRACT PUBMED 16492559

About this Structure

2FUN is a Protein complex structure of sequences from Autographa californica nucleopolyhedrovirus and Homo sapiens. Full crystallographic information is available from OCA.

Reference

Native chemical ligation in covalent caspase inhibition by p35., Lu M, Min T, Eliezer D, Wu H, Chem Biol. 2006 Feb;13(2):117-22. PMID:16492559

Page seeded by OCA on Sun Jul 27 13:25:39 2008

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