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10.1107/S1744309112035348

http://scihub22266oqcxt.onion/10.1107/S1744309112035348
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suck abstract from ncbi


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pmid23027747      Acta+Crystallogr+Sect+F+Struct+Biol+Cryst+Commun 2012 ; 68 (Pt 10): 1198-203
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  • Purification, crystallization and preliminary crystallographic analysis of the CBS-domain pair of cyclin M2 (CNNM2) #MMPMID23027747
  • Gomez-Garcia I; Stuiver M; Ereno J; Oyenarte I; Corral-Rodriguez MA; Muller D; Martinez-Cruz LA
  • Acta Crystallogr Sect F Struct Biol Cryst Commun 2012[Oct]; 68 (Pt 10): 1198-203 PMID23027747show ga
  • 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 (Mg(2+)) wasting, which may lead to symptoms of Mg(2+) 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 A resolution, respectively, using synchrotron radiation.
  • |Animals[MESH]
  • |Cation Transport Proteins[MESH]
  • |Crystallization[MESH]
  • |Crystallography, X-Ray[MESH]
  • |Cyclins/*chemistry/isolation & purification[MESH]
  • |Humans[MESH]


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