2pfi
From Proteopedia
(New page: 200px<br /> <applet load="2pfi" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pfi, resolution 1.60Å" /> '''Crystal structure o...) |
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| - | [[Image:2pfi. | + | [[Image:2pfi.jpg|left|200px]]<br /><applet load="2pfi" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2pfi" size=" | + | |
caption="2pfi, resolution 1.60Å" /> | caption="2pfi, resolution 1.60Å" /> | ||
'''Crystal structure of the cytoplasmic domain of the human chloride channel ClC-Ka'''<br /> | '''Crystal structure of the cytoplasmic domain of the human chloride channel ClC-Ka'''<br /> | ||
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==Overview== | ==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. | 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== | ||
| - | 2PFI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with IOD and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2PFI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=IOD:'>IOD</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PFI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: cystathionine beta synthetase (cbs) domains containing protein]] | [[Category: cystathionine beta synthetase (cbs) domains containing protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:43:52 2008'' |
Revision as of 12:43, 23 January 2008
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Crystal structure of the cytoplasmic domain of the human chloride channel ClC-Ka
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.
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
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