Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5
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 transpo...
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| Veröffentlicht in: | Nature structural & molecular biology 2007-01, Vol.14 (1), p.60-67 |
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| creator | Meyer, Sebastian Savaresi, Sara Forster, Ian C Dutzler, Raimund |
| description | 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. |
| doi_str_mv | 10.1038/nsmb1188 |
| format | Article |
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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.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb1188</identifier><identifier>PMID: 17195847</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Adenine Nucleotides - metabolism ; Adenosine diphosphate ; Adenosine Diphosphate - metabolism ; Adenosine Monophosphate - metabolism ; Adenosine triphosphatase ; Adenosine Triphosphate - metabolism ; Amino Acid Sequence ; Animals ; ATP ; Binding Sites ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; Biomedical research ; Carrier proteins ; Cellular biology ; Chloride Channels - chemistry ; Chloride Channels - genetics ; Chloride Channels - metabolism ; Crystallography, X-Ray ; Dialysis ; Energy Metabolism ; Humans ; Ion channels ; Life Sciences ; Ligands ; Membrane Biology ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Mutation ; Nucleotides ; Oocytes ; Patch-Clamp Techniques ; Physiological aspects ; Protein Binding ; Protein Structure ; Protein Structure, Tertiary ; Structure ; Xenopus laevis</subject><ispartof>Nature structural & molecular biology, 2007-01, Vol.14 (1), p.60-67</ispartof><rights>Springer Nature America, Inc. 2007</rights><rights>COPYRIGHT 2007 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jan 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c540t-3e4236db70fe1de8831e0474ce6bed6ba7a793f78572ee4d5bc91c63e02253bb3</citedby><cites>FETCH-LOGICAL-c540t-3e4236db70fe1de8831e0474ce6bed6ba7a793f78572ee4d5bc91c63e02253bb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nsmb1188$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nsmb1188$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17195847$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Meyer, Sebastian</creatorcontrib><creatorcontrib>Savaresi, Sara</creatorcontrib><creatorcontrib>Forster, Ian C</creatorcontrib><creatorcontrib>Dutzler, Raimund</creatorcontrib><title>Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>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.</description><subject>Adenine Nucleotides - metabolism</subject><subject>Adenosine diphosphate</subject><subject>Adenosine Diphosphate - metabolism</subject><subject>Adenosine Monophosphate - metabolism</subject><subject>Adenosine triphosphatase</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>ATP</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedical research</subject><subject>Carrier proteins</subject><subject>Cellular biology</subject><subject>Chloride Channels - chemistry</subject><subject>Chloride Channels - genetics</subject><subject>Chloride Channels - metabolism</subject><subject>Crystallography, X-Ray</subject><subject>Dialysis</subject><subject>Energy Metabolism</subject><subject>Humans</subject><subject>Ion channels</subject><subject>Life Sciences</subject><subject>Ligands</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis</subject><subject>Mutation</subject><subject>Nucleotides</subject><subject>Oocytes</subject><subject>Patch-Clamp Techniques</subject><subject>Physiological aspects</subject><subject>Protein Binding</subject><subject>Protein Structure</subject><subject>Protein Structure, Tertiary</subject><subject>Structure</subject><subject>Xenopus 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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.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>17195847</pmid><doi>10.1038/nsmb1188</doi><tpages>8</tpages></addata></record> |
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| subjects | Adenine Nucleotides - metabolism Adenosine diphosphate Adenosine Diphosphate - metabolism Adenosine Monophosphate - metabolism Adenosine triphosphatase Adenosine Triphosphate - metabolism Amino Acid Sequence Animals ATP Binding Sites Biochemistry Biological Microscopy Biomedical and Life Sciences Biomedical research Carrier proteins Cellular biology Chloride Channels - chemistry Chloride Channels - genetics Chloride Channels - metabolism Crystallography, X-Ray Dialysis Energy Metabolism Humans Ion channels Life Sciences Ligands Membrane Biology Models, Molecular Molecular Sequence Data Mutagenesis Mutation Nucleotides Oocytes Patch-Clamp Techniques Physiological aspects Protein Binding Protein Structure Protein Structure, Tertiary Structure Xenopus laevis |
| title | Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5 |
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