2o60: Difference between revisions

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{{STRUCTURE_2o60|  PDB=2o60  |  SCENE=  }}
===Calmodulin bound to peptide from neuronal nitric oxide synthase===


==Disease==
==Calmodulin bound to peptide from neuronal nitric oxide synthase==
[[http://www.uniprot.org/uniprot/NOS1_MOUSE NOS1_MOUSE]] Note=In MDX mice (mouse model of dystrophinopathy) the dystrophin complex is disrupted and nNOS is displaced from sarcolemma and accumulates in the cytosol.
<StructureSection load='2o60' size='340' side='right'caption='[[2o60]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 
== Structural highlights ==
==Function==
<table><tr><td colspan='2'>[[2o60]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. The January 2011 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Nitric Oxide Synthase''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2011_1 10.2210/rcsb_pdb/mom_2011_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O60 FirstGlance]. <br>
[[http://www.uniprot.org/uniprot/CALM_CHICK CALM_CHICK]] 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. [[http://www.uniprot.org/uniprot/NOS1_MOUSE NOS1_MOUSE]] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Isoform NNOS Mu may be an effector enzyme for the dystrophin complex.<ref>PMID:17293453</ref>  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
 
<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=NH2:AMINO+GROUP'>NH2</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o60 OCA], [https://pdbe.org/2o60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o60 RCSB], [https://www.ebi.ac.uk/pdbsum/2o60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o60 ProSAT]</span></td></tr>
[[2o60]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. The January 2011 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Nitric Oxide Synthase''  by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2011_1 10.2210/rcsb_pdb/mom_2011_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O60 OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/CALM_CHICK CALM_CHICK] 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o6/2o60_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2o60 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Calmodulin|Calmodulin]]
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<references group="xtra"/><references/>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Nitric Oxide Synthase]]
[[Category: Nitric Oxide Synthase]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Alber, T.]]
[[Category: Alber T]]
[[Category: Ng, H L.]]
[[Category: Ng HL]]
[[Category: Wand, A J.]]
[[Category: Wand AJ]]
[[Category: Metal binding protein]]
[[Category: Protein-peptide complex]]

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