1ab8: Difference between revisions
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<StructureSection load='1ab8' size='340' side='right' caption='[[1ab8]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1ab8' size='340' side='right' caption='[[1ab8]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ab8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1ab8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AB8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AB8 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOK:FORSKOLIN'>FOK</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOK:FORSKOLIN'>FOK</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPROEX-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPROEX-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1] </span></td></tr> | ||
<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=1ab8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ab8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ab8 RCSB], [http://www.ebi.ac.uk/pdbsum/1ab8 PDBsum]</span></td></tr> | <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=1ab8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ab8 OCA], [http://pdbe.org/1ab8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ab8 RCSB], [http://www.ebi.ac.uk/pdbsum/1ab8 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1ab8" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Adenylate cyclase]] | [[Category: Adenylate cyclase]] | ||
[[Category: | [[Category: Buffalo rat]] | ||
[[Category: Hurley, J H]] | [[Category: Hurley, J H]] | ||
[[Category: Zhang, G]] | [[Category: Zhang, G]] | ||
[[Category: Adenylyl cyclase]] | [[Category: Adenylyl cyclase]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
Revision as of 04:38, 12 September 2015
RAT TYPE II ADENYLYL CYCLASE C2 DOMAIN/FORSKOLIN COMPLEXRAT TYPE II ADENYLYL CYCLASE C2 DOMAIN/FORSKOLIN COMPLEX
Structural highlights
Function[ADCY2_RAT] This is a membrane-bound, calmodulin-insensitive adenylyl cyclase. 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 PubMedMammalian adenylyl cyclases contain two conserved regions, C1 and C2, which are responsible for forskolin- and G-protein-stimulated catalysis. The structure of the C2 catalytic region of type II rat adenylyl cyclase has an alpha/beta class fold in a wreath-like dimer, which has a central cleft. Two forskolin molecules bind in hydrophobic pockets at the ends of cleft. The central part of the cleft is lined by charged residues implicated in ATP binding. Forskolin appears to activate adenylyl cyclase by promoting the assembly of the active dimer and by direct interaction within the catalytic cleft. Other adenylyl cyclase regulators act at the dimer interface or on a flexible C-terminal region. Structure of the adenylyl cyclase catalytic core.,Zhang G, Liu Y, Ruoho AE, Hurley JH Nature. 1997 Mar 20;386(6622):247-53. PMID:9069282[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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