2q7o: Difference between revisions
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==Structure of human purine nucleoside phosphorylase in complex with L-Immucillin-H== | ==Structure of human purine nucleoside phosphorylase in complex with L-Immucillin-H== | ||
<StructureSection load='2q7o' size='340' side='right' caption='[[2q7o]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='2q7o' size='340' side='right' caption='[[2q7o]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NP, PNP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NP, PNP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Purine-nucleoside_phosphorylase Purine-nucleoside phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.1 2.4.2.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Purine-nucleoside_phosphorylase Purine-nucleoside phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.1 2.4.2.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q7o OCA], [http://pdbe.org/2q7o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q7o RCSB], [http://www.ebi.ac.uk/pdbsum/2q7o PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q7o OCA], [http://pdbe.org/2q7o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q7o RCSB], [http://www.ebi.ac.uk/pdbsum/2q7o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q7o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2q7o" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2q7o" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:40, 18 October 2017
Structure of human purine nucleoside phosphorylase in complex with L-Immucillin-HStructure of human purine nucleoside phosphorylase in complex with L-Immucillin-H
Structural highlights
Disease[PNPH_HUMAN] Defects in PNP are the cause of purine nucleoside phosphorylase deficiency (PNPD) [MIM:613179]. It leads to a severe T-cell immunodeficiency with neurologic disorder in children.[1] [2] [3] Function[PNPH_HUMAN] The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.[4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman purine nucleoside phosphorylase (PNP) was crystallized with transition-state analogue inhibitors Immucillin-H and DADMe-Immucillin-H synthesized with ribosyl mimics of l-stereochemistry. The inhibitors demonstrate that major driving forces for tight binding of these analogues are the leaving group interaction and the cationic mimicry of the transition state, even though large geometric changes occur with d-Immucillins and l-Immucillins bound to human PNP. L-Enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase.,Rinaldo-Matthis A, Murkin AS, Ramagopal UA, Clinch K, Mee SP, Evans GB, Tyler PC, Furneaux RH, Almo SC, Schramm VL J Am Chem Soc. 2008 Jan 23;130(3):842-4. Epub 2007 Dec 23. PMID:18154341[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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