2c3e: Difference between revisions

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==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 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.

==About this Structure==

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[[Category: transport protein]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:44:34 2008''

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@@ Line 4: / Line 4: @@
 ==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 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.
 ==About this Structure==
@@ Line 26: / Line 26: @@
 [[Category: transport protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:30:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:44:34 2008''