1t9r
From Proteopedia
(Difference between revisions)
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<StructureSection load='1t9r' size='340' side='right'caption='[[1t9r]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1t9r' size='340' side='right'caption='[[1t9r]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1t9r]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1t9r]] is a 1 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=1T9R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T9R FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1t9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t9r OCA], [https://pdbe.org/1t9r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t9r RCSB], [https://www.ebi.ac.uk/pdbsum/1t9r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t9r ProSAT]</span></td></tr> | |
- | + | ||
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/PDE5A_HUMAN PDE5A_HUMAN] Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. |
== 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=1t9r 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=1t9r ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Phosphodiesterases (PDEs) comprise a family of enzymes that modulate the immune response, inflammation, and memory, among many other functions. There are three types of PDEs: cAMP-specific, cGMP-specific, and dual-specific. Here we describe the mechanism of nucleotide selectivity on the basis of high-resolution co-crystal structures of the cAMP-specific PDE4B and PDE4D with AMP, the cGMP-specific PDE5A with GMP, and the apo-structure of the dual-specific PDE1B. These structures show that an invariant glutamine functions as the key specificity determinant by a "glutamine switch" mechanism for recognizing the purine moiety in cAMP or cGMP. The surrounding residues anchor the glutamine residue in different orientations for cAMP and for cGMP. The PDE1B structure shows that in dual-specific PDEs a key histidine residue may enable the invariant glutamine to toggle between cAMP and cGMP. The structural understanding of nucleotide binding enables the design of new PDE inhibitors that may treat diseases in which cyclic nucleotides play a critical role. | ||
- | |||
- | A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases.,Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G Mol Cell. 2004 Jul 23;15(2):279-86. PMID:15260978<ref>PMID:15260978</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1t9r" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]] | *[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
- | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Artis | + | [[Category: Artis DR]] |
- | [[Category: Bollag | + | [[Category: Bollag G]] |
- | [[Category: Card | + | [[Category: Card GL]] |
- | [[Category: Fong | + | [[Category: Fong D]] |
- | [[Category: Gillette | + | [[Category: Gillette S]] |
- | [[Category: Hsieh | + | [[Category: Hsieh D]] |
- | [[Category: Kim | + | [[Category: Kim S-H]] |
- | [[Category: Milburn | + | [[Category: Milburn MV]] |
- | [[Category: Neiman | + | [[Category: Neiman J]] |
- | [[Category: Schlessinger | + | [[Category: Schlessinger J]] |
- | [[Category: Suzuki | + | [[Category: Suzuki Y]] |
- | [[Category: West | + | [[Category: West BL]] |
- | [[Category: Zhang | + | [[Category: Zhang C]] |
- | [[Category: Zhang | + | [[Category: Zhang KYJ]] |
- | + | ||
- | + |
Current revision
Catalytic Domain Of Human Phosphodiesterase 5A
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Categories: Homo sapiens | Large Structures | Artis DR | Bollag G | Card GL | Fong D | Gillette S | Hsieh D | Kim S-H | Milburn MV | Neiman J | Schlessinger J | Suzuki Y | West BL | Zhang C | Zhang KYJ