2wey: Difference between revisions
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<StructureSection load='2wey' size='340' side='right'caption='[[2wey]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='2wey' size='340' side='right'caption='[[2wey]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wey]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2wey]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WEY FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EV1:1-(3,4-DIMETHOXYBENZYL)-6,7-DIMETHOXYISOQUINOLINE'>EV1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EV1:1-(3,4-DIMETHOXYBENZYL)-6,7-DIMETHOXYISOQUINOLINE'>EV1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lrb|1lrb]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lrb|1lrb]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wey OCA], [https://pdbe.org/2wey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wey RCSB], [https://www.ebi.ac.uk/pdbsum/2wey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wey ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
*[[Phosphodiesterase|Phosphodiesterase]] | *[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:54, 7 July 2021
Human PDE-papaverine complex obtained by ligand soaking of cross- linked protein crystalsHuman PDE-papaverine complex obtained by ligand soaking of cross- linked protein crystals
Structural highlights
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 PubMedProtein crystallography has proven to be an effective method of obtaining high-resolution structures of protein-ligand complexes. However, in certain cases only apoprotein structures are readily available and the generation of crystal complexes is more problematic. Some crystallographic systems are not amenable to soaking of ligands owing to crystal-packing effects and many protein-ligand complexes do not crystallize under the same conditions as used for the apoprotein. Using crystals of human phosphodiesterase 10a (hPDE10a) as an example of such a challenging crystallographic system, the structure of the complex with papaverine was obtained to 2.8 A resolution using protein crystals cross-linked by glutaraldehyde prior to soaking of the ligand. Inspection of the electron-density maps suggested that the correct mode of binding was obtained in one of the two monomers in the asymmetric unit and inspection of crystal-packing contacts explained why cocrystallization experiments and soaking of crystals that were not cross-linked were unsuccessful. Cross-linking of protein crystals as an aid in the generation of binary protein-ligand crystal complexes, exemplified by the human PDE10a-papaverine structure.,Andersen OA, Schonfeld DL, Toogood-Johnson I, Felicetti B, Albrecht C, Fryatt T, Whittaker M, Hallett D, Barker J Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):872-4. Epub 2009, Jul 17. PMID:19622871[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Human
- Large Structures
- Albrecht, C
- Andersen, O A
- Barker, J
- Felicetti, B
- Fryatt, T
- Hallett, D
- Schonfeld, D L
- Toogood-Johnson, I
- Whittaker, M
- Allosteric enzyme
- Alternative splicing
- Camp
- Camp-binding
- Cgmp
- Cgmp-binding
- Cross-linking
- Cytoplasm
- Hydrolase
- Magnesium
- Metal-binding
- Nucleotide-binding
- Papaverine
- Phosphodiesterase
- Phosphoprotein
- Polymorphism
- Zinc