2j9l: Difference between revisions

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[[Image:2j9l.~~jpg~~|left|200px]]

[[Image:2j9l.png|left|200px]]

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~~'''~~CYTOPLASMIC DOMAIN OF THE HUMAN CHLORIDE TRANSPORTER CLC-5 IN COMPLEX WITH ATP~~'''~~

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

~~==Overview==~~

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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 line below this paragraph, {{ABSTRACT_PUBMED_17195847}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17195847 is the PubMed ID number.

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==About this Structure==

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[[Category: Transport]]

[[Category: Voltage-gated channel]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 08~~:33:42 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:44:53 2008''

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-[[Image:2j9l.jpg|left|200px]]
+{{Seed}}
+[[Image:2j9l.png|left|200px]]
 <!--
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 {{STRUCTURE_2j9l|  PDB=2j9l  |  SCENE=  }}
-'''CYTOPLASMIC DOMAIN OF THE HUMAN CHLORIDE TRANSPORTER CLC-5 IN COMPLEX WITH ATP'''
+===CYTOPLASMIC DOMAIN OF THE HUMAN CHLORIDE TRANSPORTER CLC-5 IN COMPLEX WITH ATP===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_17195847}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17195847 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17195847}}
 ==About this Structure==
@@ Line 39: / Line 43: @@
 [[Category: Transport]]
 [[Category: Voltage-gated channel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 08:33:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:44:53 2008''