| Literature DB >> 16511206 |
Youssef Ben Ammar1, Soichi Takeda, Mitsuaki Sugawara, Masashi Miyano, Hidezo Mori, Shigeo 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 A and belong to a tetragonal space group, with unit-cell parameters a = b = 49.96, c = 103.20 A.Entities:
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Year: 2005 PMID: 16511206 PMCID: PMC1991313 DOI: 10.1107/S1744309105030836
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091