Crystal structure of human soluble calcium-activated nucleotidase (SCAN) with calcium ionCrystal structure of human soluble calcium-activated nucleotidase (SCAN) with calcium ion
Structural highlights
2h2n is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
CANT1_HUMAN Desbuquois syndrome. The disease is caused by mutations affecting the gene represented in this entry.
Function
CANT1_HUMAN Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.[1][2][3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
↑Smith TM, Hicks-Berger CA, Kim S, Kirley TL. Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. PMID:12234496
↑Yang M, Kirley TL. Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1): identification of residues essential for enzyme activity and the Ca(2+)-induced conformational change. Biochemistry. 2004 Jul 20;43(28):9185-94. PMID:15248776 doi:http://dx.doi.org/10.1021/bi049565o
↑Nizon M, Huber C, De Leonardis F, Merrina R, Forlino A, Fradin M, Tuysuz B, Abu-Libdeh BY, Alanay Y, Albrecht B, Al-Gazali L, Basaran SY, Clayton-Smith J, Desir J, Gill H, Greally MT, Koparir E, van Maarle MC, MacKay S, Mortier G, Morton J, Sillence D, Vilain C, Young I, Zerres K, Le Merrer M, Munnich A, Le Goff C, Rossi A, Cormier-Daire V. Further delineation of CANT1 phenotypic spectrum and demonstration of its role in proteoglycan synthesis. Hum Mutat. 2012 Aug;33(8):1261-6. doi: 10.1002/humu.22104. Epub 2012 May 22. PMID:22539336 doi:http://dx.doi.org/10.1002/humu.22104