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[[Image:2hqw.jpg|left|200px]]


{{Structure
==Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide==
|PDB= 2hqw |SIZE=350|CAPTION= <scene name='initialview01'>2hqw</scene>, resolution 1.90&Aring;
<StructureSection load='2hqw' size='340' side='right'caption='[[2hqw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
<table><tr><td colspan='2'>[[2hqw]] is a 2 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=2HQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HQW FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE= Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
<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>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hqw OCA], [https://pdbe.org/2hqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hqw RCSB], [https://www.ebi.ac.uk/pdbsum/2hqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hqw ProSAT]</span></td></tr>
</table>
== Function ==
[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]
== 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/hq/2hqw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2hqw ConSurf].
<div style="clear:both"></div>


'''Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide'''
==See Also==
 
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Calmodulin (CaM) regulates tetrameric N-methyl-D-aspartate receptors (NMDARs) by binding tightly to the C0 and C1 regions of its NR1 subunit. A crystal structure (2HQW; 1.96 A) of calcium-saturated CaM bound to NR1C1 (peptide spanning 875-898) showed that NR1 S890, whose phosphorylation regulates membrane localization, was solvent protected, whereas the endoplasmic reticulum retention motif was solvent exposed. NR1 F880 filled the CaM C-domain pocket, whereas T886 was closest to the N-domain pocket. This 1-7 pattern was most similar to that in the CaM-MARCKS complex. Comparison of CaM-ligand wrap-around conformations identified a core tetrad of CaM C-domain residues (FLMM(C)) that contacted all ligands consistently. An identical tetrad of N-domain residues (FLMM(N)) made variable sets of contacts with ligands. This CaM-NR1C1 structure provides a foundation for designing mutants to test the role of CaM in NR1 trafficking as well as insights into how the homologous CaM domains have different roles in molecular recognition.
[[Category: Homo sapiens]]
 
[[Category: Large Structures]]
==About this Structure==
2HQW 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=2HQW OCA].
 
==Reference==
The NMDA receptor NR1 C1 region bound to calmodulin: structural insights into functional differences between homologous domains., Ataman ZA, Gakhar L, Sorensen BR, Hell JW, Shea MA, Structure. 2007 Dec;15(12):1603-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18073110 18073110]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Akyol, Z.]]
[[Category: Akyol Z]]
[[Category: Gakhar, L.]]
[[Category: Gakhar L]]
[[Category: Hell, J H.]]
[[Category: Hell JH]]
[[Category: Shea, M A.]]
[[Category: Shea MA]]
[[Category: Sorensen, B R.]]
[[Category: Sorensen BR]]
[[Category: CA]]
[[Category: alternative splicing]]
[[Category: c1 casette]]
[[Category: calcium channel]]
[[Category: calmodulin]]
[[Category: central nervous system]]
[[Category: ef hand motif]]
[[Category: er retention signal]]
[[Category: globular complex]]
[[Category: glutamate]]
[[Category: ion channel]]
[[Category: metal binding protein]]
[[Category: n-methyl-d-aspartate receptor]]
[[Category: neuronal channel]]
[[Category: nr1]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:20:27 2008''

Latest revision as of 09:34, 14 February 2024

Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide

2hqw, resolution 1.90Å

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