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Inosine monophosphate dehydrogenase: Difference between revisions

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<StructureSection load='Figure_2.pdb' size='350' side='right' scene='Journal:JBSD:1/Cv/1' caption=''>
<StructureSection load='Figure_2.pdb' size='350' side='right' scene='Journal:JBSD:1/Cv/1' caption='Human IMPDH ([[1b3o]])'>


== Function ==
== Function ==
Line 35: Line 35:


Stereospecific interaction or recognition of IN to C2 domain through <scene name='Journal:JBSD:1/Cv/12'>conserved water mediated salt bridge (K109 (NZ) --- D215 / D216 and K109 (NZ) --- WII1 --- D215 / D216)</scene> are observed to be unique in hIMPDH–II, which is not observed in type I isoform (1JCN). The geometrical and electronic consequences of <scene name='Journal:JBSD:1/Cv/14'>conserved water molecular interaction as shown in Figure 5 (K109 to acidic D215 / D216 and E217)</scene> and their stereo chemical features (specially in CBS --- IN inter-domain recognition site) may be used to design the actual topology of inhibitor for hIMPDH-II isoform using water mimic inhibitor design protocol. Possibly, heterocyclic ligand with flexible structure containing two or three basic and hydrophilic groups with suitable spacer length may be implemented to design the isoform selective inhibitor for CML cancer.
Stereospecific interaction or recognition of IN to C2 domain through <scene name='Journal:JBSD:1/Cv/12'>conserved water mediated salt bridge (K109 (NZ) --- D215 / D216 and K109 (NZ) --- WII1 --- D215 / D216)</scene> are observed to be unique in hIMPDH–II, which is not observed in type I isoform (1JCN). The geometrical and electronic consequences of <scene name='Journal:JBSD:1/Cv/14'>conserved water molecular interaction as shown in Figure 5 (K109 to acidic D215 / D216 and E217)</scene> and their stereo chemical features (specially in CBS --- IN inter-domain recognition site) may be used to design the actual topology of inhibitor for hIMPDH-II isoform using water mimic inhibitor design protocol. Possibly, heterocyclic ligand with flexible structure containing two or three basic and hydrophilic groups with suitable spacer length may be implemented to design the isoform selective inhibitor for CML cancer.
</StructureSection>


==3D structures of inosine monophosphate dehydrogenase==
==3D structures of inosine monophosphate dehydrogenase==
[[Inosine monophosphate dehydrogenase 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*IMPDH
 
**[[1ak5]] – TfIMPDH – ''Tritrichomonas foetus'' <br />
**[[1eep]] – IMPDH – ''Borellia burgdorferi'' <br />
**[[1zfj]] – IMPDH catalytic domain – ''Streptococcus pyogenes'' <br />
**[[1vrd]] – IMPDH – ''Thermotoga maritima'' <br />
**[[3ffs]] – CpIMPDH – ''Cryptosporidium parvum''<br />
**[[3r2g]] – IMPDH – ''Legionella pneumophila'' <br />
**[[3tsb]], [[4mjm]], [[4myx]] – BaIMPDH (mutant) – ''Bacillus anthracis'' <br />
**[[4fez]] – VcIMPDH – ''Vibrio cholerae'' <br />
**[[4avf]], [[3zfh]] – PaIMPDH – ''Pseudomonas aeruginosa'' <br />
 
*IMPDH binary complex
 
**[[1me8]] – TfIMPDH + ribavirin monophosphate  <br />
**[[1pvn]] – TfIMPDH catalytic domain + transition state analog <br />
**[[1me9]] – TfIMPDH + inosinic acid <br />
**[[2cu0]] – IMPDH + xanthosine monophosphate – ''Pyrococcus horikoshii''<br />
**[[3tsd]] – BaIMPDH (mutant) + xanthosine monophosphate <br />
**[[3usb]] – BaIMPDH + inosinic acid <br />
**[[4ix2]] – VcIMPDH + inosinic acid <br />
**[[4qq3]] – VcIMPDH (mutant) + XMP <br />
**[[4dqw]] – PaIMPDH + ATP <br />
**[[1jcn]] – hMPDH 1 + IMP derivative - human<br />
**[[1jr1]] – hMPDH 2 + mycophenolic acid <br />
**[[4r7j]] – CjIMPDH catalytic domain (mutant) + inosinic acid – ''Campylobacter jejuni''<br />
 
*IMPDH ternary complex
 
**[[1me7]] – TfIMPDH + ribavirin monophosphate + mycophenolic acid <br />
**[[1lrt]] – TfIMPDH + adenine derivative + inosinic acid <br />
**[[1meh]] – TfIMPDH + mycophenolic acid + inosinic acid <br />
**[[1mei]] – TfIMPDH + mycophenolic acid + xanthosine monophosphate <br />
**[[1mew]] – TfIMPDH + NAD + xanthosine monophosphate <br />
**[[4fo4]], [[4fxs]] – VcIMPDH + mycophenolic acid + inosinic acid <br />
**[[4hlv]] – VcIMPDH + NAD + inosinic acid <br />
**[[4qne]] – VcIMPDH (mutant) + NAD + IMP <br />
**[[4x3z]] – VcIMPDH (mutant) + NAD + XMP <br />
**[[4ixh]], [[3khj]], [[4qj1]] – CpIMPDH catalytic domain + inhibitor + inosinic acid <br />
**[[4rv8]] - CpIMPDH catalytic domain (mutant) + inhibitor + inosinic acid <br />
**[[4my1]], [[4mya]], [[4mxs]], [[4my9]], [[4qm1]] – BaIMPDH catalytic domain (mutant) + inhibitor + inosinic acid <br />
**[[4mz1]], [[4mz8]] – CjIMPDH catalytic domain (mutant) + inhibitor + inosinic acid <br />
**[[4q32]], [[4q33]] – MPDH + IMP + inhibitor – ''Clostridium perfringens'' <br />
**[[4af0]] – IMPDH + mycophenolic acid + inosinic acid – ''Cryptococcus neoformans''<br />
**[[1b3o]] – hMPDH 2 + selenazole inhibitor + IMP derivative <br />
**[[1nfb]] – hMPDH 2 + NAD + IMP derivative <br />
**[[1nf7]] – hMPDH 2 + mycophenolic adenine dinucleotide + ribavirin monophosphate <br />


}}
== References ==
== References ==
<references/>
<references/>


[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky
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