Crystallization and preliminary crystallographic analysis of the human calcineurin homologous protein CHP2 bound to the cytoplasmic region of the Na+/H+ exchanger NHE1.
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.
Ben Ammar
Youssef
Y
Department of Molecular Physiology, National Cardiovascular Center Research Institute, Fujishiro-dai 5-7-1, Suita, Osaka 565-8565, Japan.
Takeda
Soichi
S
Sugawara
Mitsuaki
M
Miyano
Masashi
M
Mori
Hidezo
H
Wakabayashi
Shigeo
S
D019703:Calcineurin / Q000737:chemistry; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D027682:Cation Transport Proteins / Q000737:chemistry*; D002462:Cell Membrane / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D003593:Cytoplasm / Q000378:metabolism; D004058:Diffusion; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry; D020033:Protein Isoforms; D017434:Protein Structure, Tertiary; D000074082:Sodium-Hydrogen Exchanger 1; D017923:Sodium-Hydrogen Exchangers / Q000737:chemistry*; D013696:Temperature
C469743:CHP1 protein, human; D002135:Calcium-Binding Proteins; D027682:Cation Transport Proteins; D008565:Membrane Proteins; D020033:Protein Isoforms; C490998:SLC9A1 protein, human; D000074082:Sodium-Hydrogen Exchanger 1; D017923:Sodium-Hydrogen Exchangers; D011092:Polyethylene Glycols; D019703:Calcineurin