2c3e

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{{STRUCTURE_2c3e| PDB=2c3e | SCENE= }}
{{STRUCTURE_2c3e| PDB=2c3e | SCENE= }}
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'''THE BOVINE MITOCHONDRIAL ADP-ATP CARRIER'''
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===THE BOVINE MITOCHONDRIAL ADP-ATP CARRIER===
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==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.
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{{ABSTRACT_PUBMED_16226253}}
==About this Structure==
==About this Structure==
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[[Category: Nucleotide transport]]
[[Category: Nucleotide transport]]
[[Category: Transport protein]]
[[Category: Transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:00:33 2008''

Revision as of 19:00, 28 July 2008

Image:2c3e.png

Template:STRUCTURE 2c3e

THE BOVINE MITOCHONDRIAL ADP-ATP CARRIER

Template:ABSTRACT PUBMED 16226253

About this Structure

2C3E is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers., Nury H, Dahout-Gonzalez C, Trezeguet V, Lauquin G, Brandolin G, Pebay-Peyroula E, FEBS Lett. 2005 Nov 7;579(27):6031-6. Epub 2005 Oct 6. PMID:16226253

Page seeded by OCA on Mon Jul 28 22:00:33 2008

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