Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 10 (October 2005)

crystallization communications


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Acta Cryst. (2005). F61, 956-958    [ doi:10.1107/S1744309105030836 ]

Crystallization and preliminary crystallographic analysis of the human calcineurin homologous protein CHP2 bound to the cytoplasmic region of the Na+/H+ exchanger NHE1

Y. Ben Ammar, S. Takeda, M. Sugawara, M. Miyano, H. Mori and S. Wakabayashi

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 Å and belong to a tetragonal space group, with unit-cell parameters a = b = 49.96, c = 103.20 Å.

Keywords: calcineurin homologous proteins; Na+/H+ exchangers.

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