2j9l: Difference between revisions

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==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.

==Disease==

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[[Category: Single protein]]

[[Category: Dutzler, R.]]

[[Category: Forster, I.C.]]

[[Category: Forster, I C.]]

[[Category: Meyer, S.]]

[[Category: Savaresi, S.]]

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[[Category: voltage-gated channel]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:00:48 2008''

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@@ Line 4: / Line 4: @@
 ==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.
 ==Disease==
@@ Line 17: / Line 17: @@
 [[Category: Single protein]]
 [[Category: Dutzler, R.]]
-[[Category: Forster, I.C.]]
+[[Category: Forster, I C.]]
 [[Category: Meyer, S.]]
 [[Category: Savaresi, S.]]
@@ Line 36: / Line 36: @@
 [[Category: voltage-gated channel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:43:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:00:48 2008''