2ja3

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ja3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ja3 OCA], [http://www.ebi.ac.uk/pdbsum/2ja3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ja3 RCSB]</span>
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==Overview==
==Overview==
The ubiquitous CBS domains, which are found as part of cytoplasmic domains in the ClC family of chloride channels and transporters, have previously been identified as building blocks for regulatory nucleotide-binding sites. Here we report the structures of the cytoplasmic domain of the human transporter ClC-5 in complex with ATP and ADP. The nucleotides bind to a specific site in the protein. As determined by equilibrium dialysis, the affinities for ATP, ADP and AMP are in the high micromolar range. Point mutations that interfere with nucleotide binding change the transport behavior of a ClC-5 mutant expressed in Xenopus laevis oocytes. Our results establish the structural and energetic basis for the interaction of ClC-5 with nucleotides and provide a framework for future investigations.
The ubiquitous CBS domains, which are found as part of cytoplasmic domains in the ClC family of chloride channels and transporters, have previously been identified as building blocks for regulatory nucleotide-binding sites. Here we report the structures of the cytoplasmic domain of the human transporter ClC-5 in complex with ATP and ADP. The nucleotides bind to a specific site in the protein. As determined by equilibrium dialysis, the affinities for ATP, ADP and AMP are in the high micromolar range. Point mutations that interfere with nucleotide binding change the transport behavior of a ClC-5 mutant expressed in Xenopus laevis oocytes. Our results establish the structural and energetic basis for the interaction of ClC-5 with nucleotides and provide a framework for future investigations.
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==Disease==
 
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Known diseases associated with this structure: Dent disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300008 300008]], Hypophosphatemic rickets OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300008 300008]], Nephrolithiasis, type I OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300008 300008]], Proteinuria, low molecular weight, with hypercalciuric nephrocalcinosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300008 300008]]
 
==About this Structure==
==About this Structure==
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[[Category: Meyer, S.]]
[[Category: Meyer, S.]]
[[Category: Savaresi, S.]]
[[Category: Savaresi, S.]]
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[[Category: ADP]]
 
[[Category: cbs domain]]
[[Category: cbs domain]]
[[Category: chloride]]
[[Category: chloride]]
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[[Category: voltage-gated channel]]
[[Category: voltage-gated channel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:25:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:55:12 2008''

Revision as of 00:55, 31 March 2008


PDB ID 2ja3

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, resolution 3.05Å
Sites:
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CYTOPLASMIC DOMAIN OF THE HUMAN CHLORIDE TRANSPORTER CLC-5 IN COMPLEX WITH ADP


Overview

The ubiquitous CBS domains, which are found as part of cytoplasmic domains in the ClC family of chloride channels and transporters, have previously been identified as building blocks for regulatory nucleotide-binding sites. Here we report the structures of the cytoplasmic domain of the human transporter ClC-5 in complex with ATP and ADP. The nucleotides bind to a specific site in the protein. As determined by equilibrium dialysis, the affinities for ATP, ADP and AMP are in the high micromolar range. Point mutations that interfere with nucleotide binding change the transport behavior of a ClC-5 mutant expressed in Xenopus laevis oocytes. Our results establish the structural and energetic basis for the interaction of ClC-5 with nucleotides and provide a framework for future investigations.

About this Structure

2JA3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5., Meyer S, Savaresi S, Forster IC, Dutzler R, Nat Struct Mol Biol. 2007 Jan;14(1):60-7. Epub 2006 Dec 31. PMID:17195847

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