1c15: Difference between revisions
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[[Image:1c15.gif|left|200px]] | [[Image:1c15.gif|left|200px]] | ||
'''SOLUTION STRUCTURE OF APAF-1 CARD''' | {{Structure | ||
|PDB= 1c15 |SIZE=350|CAPTION= <scene name='initialview01'>1c15</scene> | |||
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'''SOLUTION STRUCTURE OF APAF-1 CARD''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1C15 is a [ | 1C15 is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10500165 10500165] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: programmed cell death]] | [[Category: programmed cell death]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:18:31 2008'' | ||
Revision as of 08:18, 20 March 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
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