2ja3
From Proteopedia
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| - | [[Image:2ja3.jpg|left|200px]] | + | [[Image:2ja3.jpg|left|200px]] |
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| - | '''CYTOPLASMIC DOMAIN OF THE HUMAN CHLORIDE TRANSPORTER CLC-5 IN COMPLEX WITH ADP''' | + | {{Structure |
| + | |PDB= 2ja3 |SIZE=350|CAPTION= <scene name='initialview01'>2ja3</scene>, resolution 3.05Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Adp+Binding+Site+For+Chain+D'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CYTOPLASMIC DOMAIN OF THE HUMAN CHLORIDE TRANSPORTER CLC-5 IN COMPLEX WITH ADP''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2JA3 is a [ | + | 2JA3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JA3 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17195847 17195847] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: voltage-gated channel]] | [[Category: voltage-gated channel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:39:15 2008'' |
Revision as of 15:39, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CYTOPLASMIC DOMAIN OF THE HUMAN CHLORIDE TRANSPORTER CLC-5 IN COMPLEX WITH ADP
Contents |
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.
Disease
Known diseases associated with this structure: Dent disease OMIM:[300008], Hypophosphatemic rickets OMIM:[300008], Nephrolithiasis, type I OMIM:[300008], Proteinuria, low molecular weight, with hypercalciuric nephrocalcinosis OMIM:[300008]
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
Page seeded by OCA on Thu Mar 20 17:39:15 2008
Categories: Homo sapiens | Single protein | Dutzler, R. | Forster, I C. | Meyer, S. | Savaresi, S. | ADP | Cbs domain | Chloride | Chloride channel | Chloride transporter | Clc | Disease mutation | Domain | Ion transport | Ionic channel | Membrane | Transmembrane | Transport | Transport protein | Voltage-gated channel
