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2dpk

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(New page: 200px<br /><applet load="2dpk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dpk, resolution 2.50&Aring;" /> '''The Crystal Structur...)
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caption="2dpk, resolution 2.50&Aring;" />
'''The Crystal Structure of the Primary Ca2+ Sensor of the Na+/Ca2+ Exchanger'''<br />
'''The Crystal Structure of the Primary Ca2+ Sensor of the Na+/Ca2+ Exchanger'''<br />
==Overview==
==Overview==
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The Na+/Ca2+ exchanger is a plasma membrane protein that regulates, intracellular Ca2+ levels in cardiac myocytes. Transport activity is, governed by Ca2+, and the primary Ca2+ sensor (CBD1) is located in a large, cytoplasmic loop connecting two transmembrane helices. The binding of Ca2+, to the CBD1 sensory domain results in conformational changes that, stimulate the exchanger to extrude Ca2+. Here, we present a crystal, structure of CBD1 at 2.5A resolution, which reveals a novel Ca2+ binding, site consisting of four Ca2+ ions arranged in a tight planar cluster. This, intricate coordination pattern for a Ca2+ binding cluster is indicative of, a highly sensitive Ca2+ sensor and may represent a general platform for, Ca2+ sensing.
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The Na+/Ca2+ exchanger is a plasma membrane protein that regulates intracellular Ca2+ levels in cardiac myocytes. Transport activity is governed by Ca2+, and the primary Ca2+ sensor (CBD1) is located in a large cytoplasmic loop connecting two transmembrane helices. The binding of Ca2+ to the CBD1 sensory domain results in conformational changes that stimulate the exchanger to extrude Ca2+. Here, we present a crystal structure of CBD1 at 2.5A resolution, which reveals a novel Ca2+ binding site consisting of four Ca2+ ions arranged in a tight planar cluster. This intricate coordination pattern for a Ca2+ binding cluster is indicative of a highly sensitive Ca2+ sensor and may represent a general platform for Ca2+ sensing.
==About this Structure==
==About this Structure==
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2DPK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] with CA, GAI and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DPK OCA].
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2DPK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=GAI:'>GAI</scene> and <scene name='pdbligand=EPE:'>EPE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPK OCA].
==Reference==
==Reference==
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[[Category: cis-proline]]
[[Category: cis-proline]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:42:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:11 2008''

Revision as of 15:01, 21 February 2008


2dpk, resolution 2.50Å

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The Crystal Structure of the Primary Ca2+ Sensor of the Na+/Ca2+ Exchanger

Overview

The Na+/Ca2+ exchanger is a plasma membrane protein that regulates intracellular Ca2+ levels in cardiac myocytes. Transport activity is governed by Ca2+, and the primary Ca2+ sensor (CBD1) is located in a large cytoplasmic loop connecting two transmembrane helices. The binding of Ca2+ to the CBD1 sensory domain results in conformational changes that stimulate the exchanger to extrude Ca2+. Here, we present a crystal structure of CBD1 at 2.5A resolution, which reveals a novel Ca2+ binding site consisting of four Ca2+ ions arranged in a tight planar cluster. This intricate coordination pattern for a Ca2+ binding cluster is indicative of a highly sensitive Ca2+ sensor and may represent a general platform for Ca2+ sensing.

About this Structure

2DPK is a Single protein structure of sequence from Canis lupus familiaris with , and as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of the primary Ca2+ sensor of the Na+/Ca2+ exchanger reveals a novel Ca2+ binding motif., Nicoll DA, Sawaya MR, Kwon S, Cascio D, Philipson KD, Abramson J, J Biol Chem. 2006 Aug 4;281(31):21577-81. Epub 2006 Jun 14. PMID:16774926

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