2wey

From Proteopedia

(Difference between revisions)

Current revision

Human PDE-papaverine complex obtained by ligand soaking of cross- linked protein crystals

Structural highlights

2wey is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PDE10_HUMAN Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate.^[1]

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 PubMed

Protein 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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wang H, Liu Y, Hou J, Zheng M, Robinson H, Ke H. Structural insight into substrate specificity of phosphodiesterase 10. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5782-7. Epub 2007 Mar 26. PMID:17389385
↑ Andersen OA, Schonfeld DL, Toogood-Johnson I, Felicetti B, Albrecht C, Fryatt T, Whittaker M, Hallett D, Barker J. Cross-linking of protein crystals as an aid in the generation of binary protein-ligand crystal complexes, exemplified by the human PDE10a-papaverine structure. Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):872-4. Epub 2009, Jul 17. PMID:19622871 doi:10.1107/S0907444909017855

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wey"

@@ Line 3: / Line 3: @@
 <StructureSection load='2wey' size='340' side='right'caption='[[2wey]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[2wey]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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" 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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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='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='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>
+== Function ==
+[https://www.uniprot.org/uniprot/PDE10_HUMAN PDE10_HUMAN] Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate.<ref>PMID:17389385</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Albrecht, C]]
+[[Category: Albrecht C]]
-[[Category: Andersen, O A]]
+[[Category: Andersen OA]]
-[[Category: Barker, J]]
+[[Category: Barker J]]
-[[Category: Felicetti, B]]
+[[Category: Felicetti B]]
-[[Category: Fryatt, T]]
+[[Category: Fryatt T]]
-[[Category: Hallett, D]]
+[[Category: Hallett D]]
-[[Category: Schonfeld, D L]]
+[[Category: Schonfeld DL]]
-[[Category: Toogood-Johnson, I]]
+[[Category: Toogood-Johnson I]]
-[[Category: Whittaker, M]]
+[[Category: Whittaker M]]
-[[Category: Allosteric enzyme]]
-[[Category: Alternative splicing]]
-[[Category: Camp]]
-[[Category: Camp-binding]]
-[[Category: Cgmp]]
-[[Category: Cgmp-binding]]
-[[Category: Cross-linking]]
-[[Category: Cytoplasm]]
-[[Category: Hydrolase]]
-[[Category: Magnesium]]
-[[Category: Metal-binding]]
-[[Category: Nucleotide-binding]]
-[[Category: Papaverine]]
-[[Category: Phosphodiesterase]]
-[[Category: Phosphoprotein]]
-[[Category: Polymorphism]]
-[[Category: Zinc]]

2wey

From Proteopedia

Current revision

Human PDE-papaverine complex obtained by ligand soaking of cross- linked protein crystals

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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