1f0j
From Proteopedia
(Difference between revisions)
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<StructureSection load='1f0j' size='340' side='right'caption='[[1f0j]], [[Resolution|resolution]] 1.77Å' scene=''> | <StructureSection load='1f0j' size='340' side='right'caption='[[1f0j]], [[Resolution|resolution]] 1.77Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1f0j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1f0j]] 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=1F0J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F0J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARS:ARSENIC'>ARS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARS:ARSENIC'>ARS</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=1f0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f0j OCA], [https://pdbe.org/1f0j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f0j RCSB], [https://www.ebi.ac.uk/pdbsum/1f0j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f0j ProSAT]</span></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=1f0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f0j OCA], [https://pdbe.org/1f0j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f0j RCSB], [https://www.ebi.ac.uk/pdbsum/1f0j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f0j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PDE4B_HUMAN PDE4B_HUMAN] Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in mediating central nervous system effects of therapeutic agents ranging from antidepressants to antiasthmatic and anti-inflammatory agents.<ref>PMID:10846163</ref> <ref>PMID:15003452</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f0j ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f0j ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Cyclic nucleotides are second messengers that are essential in vision, muscle contraction, neurotransmission, exocytosis, cell growth, and differentiation. These molecules are degraded by a family of enzymes known as phosphodiesterases, which serve a critical function by regulating the intracellular concentration of cyclic nucleotides. We have determined the three-dimensional structure of the catalytic domain of phosphodiesterase 4B2B to 1.77 angstrom resolution. The active site has been identified and contains a cluster of two metal atoms. The structure suggests the mechanism of action and basis for specificity and will provide a framework for structure-assisted drug design for members of the phosphodiesterase family. | ||
| - | |||
| - | Atomic structure of PDE4: insights into phosphodiesterase mechanism and specificity.,Xu RX, Hassell AM, Vanderwall D, Lambert MH, Holmes WD, Luther MA, Rocque WJ, Milburn MV, Zhao Y, Ke H, Nolte RT Science. 2000 Jun 9;288(5472):1822-5. PMID:10846163<ref>PMID:10846163</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1f0j" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hassell | + | [[Category: Hassell AM]] |
| - | [[Category: Holmes | + | [[Category: Holmes WD]] |
| - | [[Category: Ke | + | [[Category: Ke H]] |
| - | [[Category: Lambert | + | [[Category: Lambert MH]] |
| - | [[Category: Luther | + | [[Category: Luther MA]] |
| - | [[Category: Milburn | + | [[Category: Milburn MV]] |
| - | [[Category: Nolte | + | [[Category: Nolte RT]] |
| - | [[Category: Rocque | + | [[Category: Rocque WJ]] |
| - | [[Category: Vanderwall | + | [[Category: Vanderwall D]] |
| - | [[Category: Xu | + | [[Category: Xu RX]] |
| - | [[Category: Zhao | + | [[Category: Zhao Y]] |
| - | + | ||
| - | + | ||
Current revision
CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 4B2B
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Categories: Homo sapiens | Large Structures | Hassell AM | Holmes WD | Ke H | Lambert MH | Luther MA | Milburn MV | Nolte RT | Rocque WJ | Vanderwall D | Xu RX | Zhao Y
