2qpl: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qpl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QPL FirstGlance]. <br> | <table><tr><td colspan='2'>[[2qpl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QPL FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTY:4-AMINO-7-METHYLPYRAZOLO[1,5-A][1,3,5]TRIAZIN-2(1H)-ONE'>BTY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTY:4-AMINO-7-METHYLPYRAZOLO[1,5-A][1,3,5]TRIAZIN-2(1H)-ONE'>BTY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a9p|1a9p]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a9p|1a9p]]</td></tr> | ||
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qpl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qpl RCSB], [http://www.ebi.ac.uk/pdbsum/2qpl 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=2qpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qpl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qpl RCSB], [http://www.ebi.ac.uk/pdbsum/2qpl PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/PNPH_BOVIN PNPH_BOVIN]] 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Purine-nucleoside phosphorylase]] | [[Category: Purine-nucleoside phosphorylase]] | ||
[[Category: Berdini, V | [[Category: Berdini, V]] | ||
[[Category: Cleasby, A | [[Category: Cleasby, A]] | ||
[[Category: Garratt, R C | [[Category: Garratt, R C]] | ||
[[Category: Pereira, H M | [[Category: Pereira, H M]] | ||
[[Category: Glycosyltransferase]] | [[Category: Glycosyltransferase]] | ||
[[Category: Purine nucleoside phosphorylase]] | [[Category: Purine nucleoside phosphorylase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 00:55, 25 December 2014
Crystal structure of calf spleen purine nucleoside phosphorylase complexed to a novel purine analogueCrystal structure of calf spleen purine nucleoside phosphorylase complexed to a novel purine analogue
Structural highlights
Function[PNPH_BOVIN] 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. 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 PubMedThe combined use of a rapid virtual screen of a small fragment library together with a single point enzyme assay has been used for the discovery of novel PNP inhibitors. The availability of readily soakable crystals of bovine PNP has allowed the approach to be experimentally validated by determining the crystal structure of one of the inhibitor-PNP complexes. Comparison of the experimentally determined binding mode with that predicted by the virtual screening shows them to be similar. This represents a starting point for the growth of the ligand into a higher affinity inhibitor. Crystal structure of calf spleen purine nucleoside phosphorylase complexed to a novel purine analogue.,Pereira HM, Berdini V, Cleasby A, Garratt RC FEBS Lett. 2007 Oct 30;581(26):5082-6. Epub 2007 Oct 2. PMID:17927987[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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