Abstract
Calcineurin homologous protein (CHP) is a Ca2+-binding protein that directly interacts with and regulates the activity of all plasma-membrane Na+/H+-exchanger (NHE) family members. In contrast to the ubiquitous isoform CHP1, CHP2 is highly expressed in cancer cells. To understand the regulatory mechanism of NHE1 by CHP2, the complex CHP2-NHE1 (amino acids 503-545) has been crystallized by the sitting-drop vapour-diffusion method using PEG 3350 as precipitant. The crystals diffract to 2.7 A and belong to a tetragonal space group, with unit-cell parameters a = b = 49.96, c = 103.20 A.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Calcineurin / chemistry
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Calcium-Binding Proteins / chemistry*
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Cation Transport Proteins / chemistry*
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Cell Membrane / metabolism
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Crystallization
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Crystallography, X-Ray
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Cytoplasm / metabolism
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Diffusion
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / metabolism
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Humans
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Membrane Proteins / chemistry*
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Polyethylene Glycols / chemistry
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Protein Isoforms
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Protein Structure, Tertiary
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Sodium-Hydrogen Exchanger 1
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Sodium-Hydrogen Exchangers / chemistry*
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Temperature
Substances
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CHP1 protein, human
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Calcium-Binding Proteins
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Cation Transport Proteins
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Membrane Proteins
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Protein Isoforms
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SLC9A1 protein, human
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Sodium-Hydrogen Exchanger 1
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Sodium-Hydrogen Exchangers
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Polyethylene Glycols
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Calcineurin