1ckk

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[[Image:1ckk.jpg|left|200px]]
 
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{{Structure
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==CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT==
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|PDB= 1ckk |SIZE=350|CAPTION= <scene name='initialview01'>1ckk</scene>
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<StructureSection load='1ckk' size='340' side='right'caption='[[1ckk]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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<table><tr><td colspan='2'>[[1ckk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CKK FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= XENOPUS LAEVIS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ckk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ckk OCA], [https://pdbe.org/1ckk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ckk RCSB], [https://www.ebi.ac.uk/pdbsum/1ckk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ckk ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ckk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ckk OCA], [http://www.ebi.ac.uk/pdbsum/1ckk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ckk RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CALM1_XENLA CALM1_XENLA] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ck/1ckk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1ckk ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a 26-residue peptide, corresponding to the CaM-binding domain of rat Ca2+/CaM-dependent protein kinase kinase (CaMKK), has been determined by NMR spectroscopy. In this complex, the CaMKK peptide forms a fold comprising an alpha-helix and a hairpin-like loop whose C-terminus folds back on itself. The binding orientation of this CaMKK peptide by the two CaM domains is opposite to that observed in all other CaM-target complexes determined so far. The N- and C-terminal hydrophobic pockets of Ca2+/CaM anchor Trp 444 and Phe 459 of the CaMKK peptide, respectively. This 14-residue separation between two key hydrophobic groups is also unique among previously determined CaM complexes. The present structure represents a new and distinct class of Ca2+/CaM target recognition that may be shared by other Ca2+/CaM-stimulated proteins.
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'''CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT'''
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A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase.,Osawa M, Tokumitsu H, Swindells MB, Kurihara H, Orita M, Shibanuma T, Furuya T, Ikura M Nat Struct Biol. 1999 Sep;6(9):819-24. PMID:10467092<ref>PMID:10467092</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ckk" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a 26-residue peptide, corresponding to the CaM-binding domain of rat Ca2+/CaM-dependent protein kinase kinase (CaMKK), has been determined by NMR spectroscopy. In this complex, the CaMKK peptide forms a fold comprising an alpha-helix and a hairpin-like loop whose C-terminus folds back on itself. The binding orientation of this CaMKK peptide by the two CaM domains is opposite to that observed in all other CaM-target complexes determined so far. The N- and C-terminal hydrophobic pockets of Ca2+/CaM anchor Trp 444 and Phe 459 of the CaMKK peptide, respectively. This 14-residue separation between two key hydrophobic groups is also unique among previously determined CaM complexes. The present structure represents a new and distinct class of Ca2+/CaM target recognition that may be shared by other Ca2+/CaM-stimulated proteins.
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*[[Calcium/calmodulin-dependent protein kinase kinase|Calcium/calmodulin-dependent protein kinase kinase]]
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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==About this Structure==
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== References ==
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1CKK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKK OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase., Osawa M, Tokumitsu H, Swindells MB, Kurihara H, Orita M, Shibanuma T, Furuya T, Ikura M, Nat Struct Biol. 1999 Sep;6(9):819-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10467092 10467092]
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
 
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Furuya, T.]]
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[[Category: Furuya T]]
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[[Category: Ikura, M.]]
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[[Category: Ikura M]]
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[[Category: Kurihara, H.]]
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[[Category: Kurihara H]]
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[[Category: Orita, M.]]
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[[Category: Orita M]]
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[[Category: Osawa, M.]]
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[[Category: Osawa M]]
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[[Category: Shibanuma, T.]]
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[[Category: Shibanuma T]]
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[[Category: Swindells, M B.]]
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[[Category: Swindells MB]]
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[[Category: Tokumitsu, H.]]
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[[Category: Tokumitsu H]]
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[[Category: calmodulin]]
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[[Category: camkk]]
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[[Category: complex (calmodulin/peptide)]]
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[[Category: nmr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:23:24 2008''
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Current revision

CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT

PDB ID 1ckk

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