2c3e: Difference between revisions

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[[Image:2c3e.~~gif~~|left|200px]]

[[Image:2c3e.png|left|200px]]

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~~'''~~THE BOVINE MITOCHONDRIAL ADP-ATP CARRIER~~'''~~

===THE BOVINE MITOCHONDRIAL ADP-ATP CARRIER===

~~==Overview==~~

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The oligomerization state of the ADP/ATP carrier is an important issue in understanding the mechanism underlying nucleotide exchange across the inner mitochondrial membrane. The first high resolution structure obtained in the presence of carboxyatractyloside revealed a large cavity formed within a monomer in which the inhibitor is strongly bound. Whereas the protein-protein interactions implicated in the first crystal form are not biologically relevant, the ~~new crystal form described herein, highlights favorable protein-protein interactions. The interactions are mediated by endogenous cardiolipins, which are tightly bound~~ to the ~~protein, two cardiolipins being sandwiched between the monomers~~ on ~~the matrix side~~. ~~The putative dimerization interface evidenced here~~ is ~~consistent with other structural, biochemical or functional data published so far~~.

The line below this paragraph, {{ABSTRACT_PUBMED_16226253}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16226253 is the PubMed ID number.

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==About this Structure==

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[[Category: Nucleotide transport]]

[[Category: Transport protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 21~~:11:14 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:00:33 2008''

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-[[Image:2c3e.gif|left|200px]]
+{{Seed}}
+[[Image:2c3e.png|left|200px]]
 <!--
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 {{STRUCTURE_2c3e|  PDB=2c3e  |  SCENE=  }}
-'''THE BOVINE MITOCHONDRIAL ADP-ATP CARRIER'''
+===THE BOVINE MITOCHONDRIAL ADP-ATP CARRIER===
-==Overview==
+<!--
-The oligomerization state of the ADP/ATP carrier is an important issue in understanding the mechanism underlying nucleotide exchange across the inner mitochondrial membrane. The first high resolution structure obtained in the presence of carboxyatractyloside revealed a large cavity formed within a monomer in which the inhibitor is strongly bound. Whereas the protein-protein interactions implicated in the first crystal form are not biologically relevant, the new crystal form described herein, highlights favorable protein-protein interactions. The interactions are mediated by endogenous cardiolipins, which are tightly bound to the protein, two cardiolipins being sandwiched between the monomers on the matrix side. The putative dimerization interface evidenced here is consistent with other structural, biochemical or functional data published so far.
+The line below this paragraph, {{ABSTRACT_PUBMED_16226253}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16226253 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16226253}}
 ==About this Structure==
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 [[Category: Nucleotide transport]]
 [[Category: Transport protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:11:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:00:33 2008''