2pfi
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The cytoplasmic domains of ClC chloride channels and transporters are | + | The cytoplasmic domains of ClC chloride channels and transporters are ubiquitously found in eukaryotic family members and have been suggested to be involved in the regulation of ion transport. All cytoplasmic ClC domains share a conserved scaffold that contains a pair of CBS motifs. Here we describe the structure of the cytoplasmic component of the human chloride channel ClC-Ka at 1.6 A resolution. The structure reveals a dimeric organization of the domain that is unusual for CBS motif containing proteins. Using a biochemical approach combining mutagenesis, crosslinking, and analytical ultracentrifugation, we demonstrate that the interaction interface is preserved in solution and that the distantly related channel ClC-0 likely exhibits a similar structural organization. Our results reveal a conserved interaction interface that relates the cytoplasmic domains of ClC proteins and establish a structural relationship that is likely general for this important family of transport proteins. |
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| + | ==Disease== | ||
| + | Known disease associated with this structure: Bartter syndrome, type 4, digenic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602024 602024]] | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | The | + | The structure of the cytoplasmic domain of the chloride channel ClC-Ka reveals a conserved interaction interface., Markovic S, Dutzler R, Structure. 2007 Jun;15(6):715-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17562318 17562318] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cystathionine beta synthetase (cbs) domains containing protein]] | [[Category: cystathionine beta synthetase (cbs) domains containing protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:28:57 2008'' |
Revision as of 16:29, 21 February 2008
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Crystal structure of the cytoplasmic domain of the human chloride channel ClC-Ka
Contents |
Overview
The cytoplasmic domains of ClC chloride channels and transporters are ubiquitously found in eukaryotic family members and have been suggested to be involved in the regulation of ion transport. All cytoplasmic ClC domains share a conserved scaffold that contains a pair of CBS motifs. Here we describe the structure of the cytoplasmic component of the human chloride channel ClC-Ka at 1.6 A resolution. The structure reveals a dimeric organization of the domain that is unusual for CBS motif containing proteins. Using a biochemical approach combining mutagenesis, crosslinking, and analytical ultracentrifugation, we demonstrate that the interaction interface is preserved in solution and that the distantly related channel ClC-0 likely exhibits a similar structural organization. Our results reveal a conserved interaction interface that relates the cytoplasmic domains of ClC proteins and establish a structural relationship that is likely general for this important family of transport proteins.
Disease
Known disease associated with this structure: Bartter syndrome, type 4, digenic OMIM:[602024]
About this Structure
2PFI is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
The structure of the cytoplasmic domain of the chloride channel ClC-Ka reveals a conserved interaction interface., Markovic S, Dutzler R, Structure. 2007 Jun;15(6):715-25. PMID:17562318
Page seeded by OCA on Thu Feb 21 18:28:57 2008
