1niw

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[[Image:1niw.jpg|left|200px]]
 
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==Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin==
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The line below this paragraph, containing "STRUCTURE_1niw", creates the "Structure Box" on the page.
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<StructureSection load='1niw' size='340' side='right'caption='[[1niw]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1niw]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NIW FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
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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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1niw| PDB=1niw | SCENE= }}
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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=1niw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1niw OCA], [https://pdbe.org/1niw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1niw RCSB], [https://www.ebi.ac.uk/pdbsum/1niw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1niw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CALM1_RAT CALM1_RAT] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.[UniProtKB:P62158]
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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/ni/1niw_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=1niw ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin'''
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==See Also==
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The enzyme nitric oxide synthase (NOS) is exquisitely regulated in vivo by the Ca(2+) sensor protein calmodulin (CaM) to control production of NO, a key signaling molecule and cytotoxin. The differential activation of NOS isozymes by CaM has remained enigmatic, despite extensive research. Here, the crystallographic structure of Ca(2+)-loaded CaM bound to a 20 residue peptide comprising the endothelial NOS (eNOS) CaM-binding region establishes their individual conformations and intermolecular interactions, and suggests the basis for isozyme-specific differences. The alpha-helical eNOS peptide binds in an antiparallel orientation to CaM through extensive hydrophobic interactions. Unique NOS interactions occur with: (i). the CaM flexible central linker, explaining its importance in NOS activation; and (ii). the CaM C-terminus, explaining the NOS-specific requirement for a bulky, hydrophobic residue at position 144. This binding mode expands mechanisms for CaM-mediated activation, explains eNOS deactivation by Thr495 phosphorylation, and implicates specific hydrophobic residues in the Ca(2+) independence of inducible NOS.
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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==About this Structure==
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1NIW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA].
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==Reference==
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Structural basis for endothelial nitric oxide synthase binding to calmodulin., Aoyagi M, Arvai AS, Tainer JA, Getzoff ED, EMBO J. 2003 Feb 17;22(4):766-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12574113 12574113]
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[[Category: Nitric-oxide synthase]]
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[[Category: Protein complex]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Aoyagi, M.]]
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[[Category: Aoyagi M]]
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[[Category: Arvai, A S.]]
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[[Category: Arvai AS]]
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[[Category: Getzoff, E D.]]
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[[Category: Getzoff ED]]
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[[Category: Tainer, J A.]]
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[[Category: Tainer JA]]
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[[Category: Calcium-binding protein]]
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[[Category: Nitric oxide]]
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[[Category: No]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:35:16 2008''
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Current revision

Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin

PDB ID 1niw

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