1c15
From Proteopedia
(New page: 200px<br /> <applet load="1c15" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c15" /> '''SOLUTION STRUCTURE OF APAF-1 CARD'''<br /> ...) |
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| - | [[Image:1c15.gif|left|200px]]<br /> | + | [[Image:1c15.gif|left|200px]]<br /><applet load="1c15" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1c15" /> | caption="1c15" /> | ||
'''SOLUTION STRUCTURE OF APAF-1 CARD'''<br /> | '''SOLUTION STRUCTURE OF APAF-1 CARD'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Direct recruitment and activation of caspase-9 by Apaf-1 through the | + | 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== | ==About this Structure== | ||
| - | 1C15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1C15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C15 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chou, J.]] | [[Category: Chou, J.]] | ||
| - | [[Category: Olea, R | + | [[Category: Olea, R S.]] |
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
[[Category: Yuan, J.]] | [[Category: Yuan, J.]] | ||
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[[Category: programmed cell death]] | [[Category: programmed cell death]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:18 2008'' |
Revision as of 10:01, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 12:01:18 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
