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1c15
From Proteopedia
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[[Image:1c15.gif|left|200px]] | [[Image:1c15.gif|left|200px]] | ||
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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.]] | ||
| - | [[Category: | + | [[Category: Apaf]] |
| - | [[Category: | + | [[Category: Card]] |
| - | [[Category: | + | [[Category: Caspase recruitment domain]] |
| - | [[Category: | + | [[Category: Dd]] |
| - | [[Category: | + | [[Category: Ded]] |
| - | [[Category: | + | [[Category: Homophilic interaction]] |
| - | [[Category: | + | [[Category: Programmed cell death]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:12:28 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:12, 2 May 2008
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
Categories: Homo sapiens | Single protein | Chou, J. | Olea, R S. | Wagner, G. | Yuan, J. | Zhou, P. | Apaf | Card | Caspase recruitment domain | Dd | Ded | Homophilic interaction | Programmed cell death
