4ywy: Difference between revisions

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'''~~Unreleased structure~~'''

==Crystal Structure of double mutant Y115E Y117E human Glutaminyl Cyclase in complex with inhibitor PBD-150==

~~The entry~~ 4ywy is ~~ON HOLD~~

== Structural highlights ==

<table><tr><td colspan='2'>[[4ywy]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YWY OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YWY FirstGlance].

~~Authors~~: ~~Di Pisa~~, F., ~~Pozzi~~, C., ~~Benvenuti~~, M., ~~Mangani~~, S.

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PBD:1-(3,4-DIMETHOXYPHENYL)-3-[3-(1H-IMIDAZOL-1-YL)PROPYL]THIOUREA'>PBD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </td></tr>

~~Description~~: ~~Crystal Structure~~ of ~~double mutant Y115E Y117E human Glutaminyl Cyclase~~ in ~~complex with inhibitor PBD~~-~~150~~

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ywy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ywy RCSB], [http://www.ebi.ac.uk/pdbsum/4ywy PDBsum]</td></tr>

[[Category: ~~Unreleased Structures~~]]

</table>

== Function ==

[[http://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN]] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>

== References ==

__TOC__

</StructureSection>

[[Category: Glutaminyl-peptide cyclotransferase]]

[[Category: Benvenuti, M]]

[[Category: Mangani, S]]

[[Category: Pisa, F Di]]

[[Category: Pozzi, C]]

[[Category: ~~Mangani, S~~]]

[[Category: Alzheimer disease]]

[[Category: ~~Di Pisa, F~~]]

[[Category: Cyclotransferase soluble variant]]

[[Category: Pbd-150 inhibitor]]

[[Category: Transferase]]

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-'''Unreleased structure'''
+==Crystal Structure of double mutant Y115E Y117E human Glutaminyl Cyclase in complex with inhibitor PBD-150==
+<StructureSection load='4ywy' size='340' side='right' caption='[[4ywy]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
-The entry 4ywy is ON HOLD
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4ywy]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YWY FirstGlance]. <br>
-Authors: Di Pisa, F., Pozzi, C., Benvenuti, M., Mangani, S.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PBD:1-(3,4-DIMETHOXYPHENYL)-3-[3-(1H-IMIDAZOL-1-YL)PROPYL]THIOUREA'>PBD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></td></tr>
-Description: Crystal Structure of double mutant Y115E Y117E human Glutaminyl Cyclase in complex with inhibitor PBD-150
+<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=4ywy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ywy RCSB], [http://www.ebi.ac.uk/pdbsum/4ywy PDBsum]</span></td></tr>
-[[Category: Unreleased Structures]]
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN]] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Glutaminyl-peptide cyclotransferase]]
 [[Category: Benvenuti, M]]
+[[Category: Mangani, S]]
+[[Category: Pisa, F Di]]
 [[Category: Pozzi, C]]
-[[Category: Mangani, S]]
+[[Category: Alzheimer disease]]
-[[Category: Di Pisa, F]]
+[[Category: Cyclotransferase soluble variant]]
+[[Category: Pbd-150 inhibitor]]
+[[Category: Transferase]]