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Ectonucleoside triphosphate diphosphohydrolase
From Proteopedia
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| - | <StructureSection load='4brg' size=' | + | <StructureSection load='4brg' size='400' side='right' caption='Structure of NTDPase1 complex with GMPPNP, Na+ (purple), Cl- (large green), Mg+2 (small green) ions (PDB code [[4brg]]).' scene='59/597004/Cv/1'> |
| - | == Function == | ||
'''Ectonucleoside triphosphate diphosphohydrolase (NTPDase)''' hydrolyzes nucleoside 5’-triphosphate to nucleoside 5’-phosphate and 2 phosphates. NTPDase can hydrolyze ATP and ADP. NTPDase has an important role in regulating neutrophil chemotaxis. NTPDase 1,2,3,8 are cell surface enzymes with catalytic sites facing extracellularly while other NTPDases act intracellularly. NTPDase require Ca<sup>+2</sup> or Mg<sup>+2</sup> for their activity. The NTPDases can be differentiated according to their substrate specificity, divalent cation usage and product formation.<ref>PMID:23830739</ref> | '''Ectonucleoside triphosphate diphosphohydrolase (NTPDase)''' hydrolyzes nucleoside 5’-triphosphate to nucleoside 5’-phosphate and 2 phosphates. NTPDase can hydrolyze ATP and ADP. NTPDase has an important role in regulating neutrophil chemotaxis. NTPDase 1,2,3,8 are cell surface enzymes with catalytic sites facing extracellularly while other NTPDases act intracellularly. NTPDase require Ca<sup>+2</sup> or Mg<sup>+2</sup> for their activity. The NTPDases can be differentiated according to their substrate specificity, divalent cation usage and product formation.<ref>PMID:23830739</ref> | ||
| - | == Disease == | ||
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| - | == Relevance == | ||
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| - | == Structural highlights == | ||
</StructureSection> | </StructureSection> | ||
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**[[4a5a]], [[4kh4]] – TgNTPDase (mutant) + AMPPNP<br /> | **[[4a5a]], [[4kh4]] – TgNTPDase (mutant) + AMPPNP<br /> | ||
**[[4kh5]] – TgNTPDase (mutant) + adenosine-imido-diphosphate<br /> | **[[4kh5]] – TgNTPDase (mutant) + adenosine-imido-diphosphate<br /> | ||
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| + | *NTPDase4 | ||
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| + | **[[6wg5]] – hNTPDase <br /> | ||
}} | }} | ||
Current revision
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3D structures of ectonucleoside triphosphate diphosphohydrolase
Updated on 12-July-2021
References
- ↑ Zebisch M, Krauss M, Schafer P, Lauble P, Strater N. Crystallographic Snapshots along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases. Structure. 2013 Jul 2. pii: S0969-2126(13)00200-1. doi:, 10.1016/j.str.2013.05.016. PMID:23830739 doi:10.1016/j.str.2013.05.016
