期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 68, 期 -, 页码 1198-1203出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309112035348
关键词
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资金
- Departamento de Educacion
- Universidades e Investigacion del Gobierno Vasco [PI2010-17]
- Departamento de Industria, Innovacion, Comercio y Turismo del Gobierno Vasco [ETORTEK IE05-147, IE07-202]
- Diputacion Foral de Bizkaia [Exp. 7/13/08/2006/11, 7/13/08/2005/14]
- Ministerio Espanol de Ciencia e Innovacion (MICINN) [BFU2010-17857]
- MICINN CONSOLIDER-INGENIO Program [CSD2008-00005]
- European Community [EUNEFRON 201590]
This work describes the purification and preliminary crystallographic analysis of the CBS-domain pair of the murine CNNM2 magnesium transporter (formerly known as ancient domain protein 2; ACDP2), which consists of a pair of cystathionine beta-synthase (CBS) motifs and has 100% sequence identity to its human homologue. CNNM proteins represent the least-studied members of the eight different types of magnesium transporters identified to date in mammals. In humans, the CNNM family is encoded by four genes: CNNM1-4. CNNM1 acts as a cytosolic copper chaperone, whereas CNNM2 and CNNM4 have been associated with magnesium handling. Interestingly, mutations in the CNNM2 gene cause familial dominant hypomagnesaemia (MIM:607803), a rare human disorder characterized by renal and intestinal magnesium (Mg2+) wasting, which may lead to symptoms of Mg2+ depletion such as tetany, seizures and cardiac arrhythmias. This manuscript describes the preliminary crystallographic analysis of two different crystal habits of a truncated form of the protein containing its regulatory CBS-domain pair, which has been reported to host the pathological mutation T568I in humans. The crystals belonged to space groups P2(1)2(1)2 and I222 (or I2(1)2(1)2(1)) and diffracted X-rays to 2.0 and 3.6 angstrom resolution, respectively, using synchrotron radiation.
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