Title : Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): implications for NTPDase structural modeling.

Pub. Date : 2005 Jun 28

PMID : 15966724






5 Functional Relationships(s)
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1 Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): implications for NTPDase structural modeling. Disulfides ectonucleoside triphosphate diphosphohydrolase 3 Homo sapiens
2 Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): implications for NTPDase structural modeling. Disulfides ectonucleoside triphosphate diphosphohydrolase 3 Homo sapiens
3 To investigate disulfide structure in human NTPDase3, we made single and double mutants of these 10 cysteines, and analyzed their enzymatic activity, glycosylation pattern, trafficking to the cell membrane, and sensitivity to reduction. Disulfides ectonucleoside triphosphate diphosphohydrolase 3 Homo sapiens
4 The resultant theoretical 3-D model of the extracellular portion of NTPDase3, based on homology with this exopolyphosphatase, is consistent with the assignment of the disulfide bonds occurring in regions of good fold similarity between NTPDase3 and the exopolyphosphatase. Disulfides ectonucleoside triphosphate diphosphohydrolase 3 Homo sapiens
5 The resultant theoretical 3-D model of the extracellular portion of NTPDase3, based on homology with this exopolyphosphatase, is consistent with the assignment of the disulfide bonds occurring in regions of good fold similarity between NTPDase3 and the exopolyphosphatase. Disulfides ectonucleoside triphosphate diphosphohydrolase 3 Homo sapiens