Nucleoside triphosphatase: Difference between revisions
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<StructureSection load='4a5a' size=' | <StructureSection load='4a5a' size='350' side='right' caption='NTPase 2 tetramer complex with AMPPNP and Mg++ ion (green) (PDB entry [[4a5a]])' scene=''> | ||
== Function == | == Function == | ||
'''Nucleoside triphosphatase''' or '''nucleoside triphosphate diphosphohydrolase''' (NTPase) is responsible for degradation of nucleotides to their monophosphate form. NTPase is found in mammals and in pathogenic microbes. In mammals NTPase hs a crucial role in regulation of purinergic signalling by hydrolysis of extracellular nucleotides. The function of NTPase in pathogens is still unknown<ref>PMID: | '''Nucleoside triphosphatase''' or '''nucleoside triphosphate diphosphohydrolase''' (NTPase) is responsible for degradation of nucleotides to their monophosphate form. NTPase is found in mammals and in pathogenic microbes. In mammals NTPase hs a crucial role in regulation of purinergic signalling by hydrolysis of extracellular nucleotides. The function of NTPase in pathogens is still unknown<ref>PMID:24115522</ref>. | ||
*'''Nucleoside triphosphatase Nudi''' catalyses the hydrolysis of preferentially dUTP, dTTP and dCTP. | |||
== | == Relevance == | ||
The modulation of NTPase activity sems a good therapeutic method for regulating the concentration of ATP. High ATP concentration has been shown to be involved in various disorders in the CNS including brain injury, ischemia, neuro-inflammation, epilepsy, neuropathic pain and migraine<ref>PMID:25694082</ref>. | |||
== Structural highlights == | == Structural highlights == | ||
''Toxoplasma gondii'' <snapshot name='84/844927/Cv1/3'>NTPase 2 is dimer of dimers</snapshot> (PDB code [[4a5a]]). The 3D structure of the complex between NTPase 2 and the ATP analog AMPPNP shows the NTPase structure composed of two domains. Domain I contains the N-terminal and C-terminal and domain II the core residues. The structure contains 7 Cys-Cys bonds one of which located between domain I and II and reaching the diametrically positioned monomer was found by mutational analysis to be responsible for activation. The ATP analog - AMPPNP - is located in a cleft and forms interactions with domain I and domain II<ref>PMID:22130673</ref>. | |||
*<snapshot name='84/844927/Cv1/5'>Test1</snapshot> | |||
</ | *<snapshot name='84/844927/Cv1/6'>Test2</snapshot> | ||
*<snapshot name='84/844927/Cv1/8'>Test3</snapshot> | |||
==3D structures of nucleoside triphosphatase== | ==3D structures of nucleoside triphosphatase== | ||
[[Nucleoside triphosphatase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||