1c15

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[[Image:1c15.gif|left|200px]]
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{{Structure
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{{STRUCTURE_1c15| PDB=1c15 | SCENE= }}
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|RELATEDENTRY=[[3crd|3CRD]], [[1a1w|1A1W]], [[1ddf|1DDF]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c15 OCA], [http://www.ebi.ac.uk/pdbsum/1c15 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c15 RCSB]</span>
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'''SOLUTION STRUCTURE OF APAF-1 CARD'''
'''SOLUTION STRUCTURE OF APAF-1 CARD'''
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[[Category: Yuan, J.]]
[[Category: Yuan, J.]]
[[Category: Zhou, P.]]
[[Category: Zhou, P.]]
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[[Category: apaf]]
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[[Category: Apaf]]
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[[Category: card]]
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[[Category: Card]]
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[[Category: caspase recruitment domain]]
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[[Category: Caspase recruitment domain]]
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[[Category: dd]]
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[[Category: Dd]]
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[[Category: ded]]
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[[Category: Ded]]
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[[Category: homophilic interaction]]
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[[Category: Homophilic interaction]]
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[[Category: programmed cell death]]
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[[Category: Programmed cell death]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:12:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:12:26 2008''
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Revision as of 09:12, 2 May 2008

Image:1c15.gif

Template:STRUCTURE 1c15

SOLUTION STRUCTURE OF APAF-1 CARD


Overview

Direct recruitment and activation of caspase-9 by Apaf-1 through the homophilic CARD/CARD (Caspase Recruitment Domain) interaction is critical for the activation of caspases downstream of mitochondrial damage in apoptosis. Here we report the solution structure of the Apaf-1 CARD domain and its surface of interaction with caspase-9 CARD. Apaf-1 CARD consists of six tightly packed amphipathic alpha-helices and is topologically similar to the RAIDD CARD, with the exception of a kink observed in the middle of the N-terminal helix. By using chemical shift perturbation data, the homophilic interaction was mapped to the acidic surface of Apaf-1 CARD centered around helices 2 and 3. Interestingly, a significant portion of the chemically perturbed residues are hydrophobic, indicating that in addition to the electrostatic interactions predicted previously, hydrophobic interaction is also an important driving force underlying the CARD/CARD interaction. On the basis of the identified functional residues of Apaf-1 CARD and the surface charge complementarity, we propose a model of CARD/CARD interaction between Apaf-1 and caspase-9.

About this Structure

1C15 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: a structural basis for specific adaptor/caspase interaction., Zhou P, Chou J, Olea RS, Yuan J, Wagner G, Proc Natl Acad Sci U S A. 1999 Sep 28;96(20):11265-70. PMID:10500165 Page seeded by OCA on Fri May 2 12:12:28 2008

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