1c15

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Revision as of 14:10, 12 November 2007

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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

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