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| | <StructureSection load='1rl3' size='340' side='right'caption='[[1rl3]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1rl3' size='340' side='right'caption='[[1rl3]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rl3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RL3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RL3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rl3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RL3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</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]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rgs|1rgs]], [[1ne4|1ne4]], [[1ne6|1ne6]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRKAR1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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=1rl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rl3 OCA], [https://pdbe.org/1rl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rl3 RCSB], [https://www.ebi.ac.uk/pdbsum/1rl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rl3 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1rl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rl3 OCA], [http://pdbe.org/1rl3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rl3 RCSB], [http://www.ebi.ac.uk/pdbsum/1rl3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rl3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KAP0_BOVIN KAP0_BOVIN]] Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. | + | [https://www.uniprot.org/uniprot/KAP0_BOVIN KAP0_BOVIN] Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brown, S]] | + | [[Category: Brown S]] |
| - | [[Category: Taylor, S S]] | + | [[Category: Taylor SS]] |
| - | [[Category: Wu, J]] | + | [[Category: Wu J]] |
| - | [[Category: Xuong, N H]] | + | [[Category: Xuong N-H]] |
| - | [[Category: Camp-dependent protein kinase]]
| + | |
| - | [[Category: Camp-free]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Type 1a regulatory subunit]]
| + | |
| Structural highlights
Function
KAP0_BOVIN Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
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
In eukaryotes the primary target for cAMP, a ubiquitous second messenger, is cAMP-dependent protein kinase (PKA). Understanding how binding and release of cAMP changes the cAMP binding domains and then triggers long-range allosteric responses is an important challenge. This conformational switching requires structure solutions of cAMP binding domains in cAMP-bound and cAMP-free states. We describe for the first time a crystal structure of the cAMP binding domains of PKA type Ialpha regulatory subunit where site A is occupied by cGMP and site B is unoccupied. The structure reveals that the carboxyl terminus of domain B serves as a hydrophobic cap, locking the cyclic nucleotide via its adenine ring into the beta-barrel. In the absence of cAMP, the "cap" is released via an extension of the C-terminal helix. This simple hinge mechanism for binding and release of cAMP also provides a mechanism for allosteric communication between sites A and B.
RIalpha subunit of PKA: a cAMP-free structure reveals a hydrophobic capping mechanism for docking cAMP into site B.,Wu J, Brown S, Xuong NH, Taylor SS Structure. 2004 Jun;12(6):1057-65. PMID:15274925[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wu J, Brown S, Xuong NH, Taylor SS. RIalpha subunit of PKA: a cAMP-free structure reveals a hydrophobic capping mechanism for docking cAMP into site B. Structure. 2004 Jun;12(6):1057-65. PMID:15274925 doi:10.1016/j.str.2004.03.022
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