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[[Image:1np8.jpg|left|200px]]


{{Structure
==18-k C-terminally trunucated small subunit of calpain==
|PDB= 1np8 |SIZE=350|CAPTION= <scene name='initialview01'>1np8</scene>, resolution 2.00&Aring;
<StructureSection load='1np8' size='340' side='right'caption='[[1np8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>
<table><tr><td colspan='2'>[[1np8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NP8 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]] 2&#8491;</td></tr>
|GENE= CAPNS1 OR CAPN4 OR CSS1 ([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=CD:CADMIUM+ION'>CD</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1np8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1np8 OCA], [https://pdbe.org/1np8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1np8 RCSB], [https://www.ebi.ac.uk/pdbsum/1np8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1np8 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1np8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1np8 OCA], [http://www.ebi.ac.uk/pdbsum/1np8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1np8 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/CPNS1_RAT CPNS1_RAT] Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
== 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/np/1np8_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=1np8 ConSurf].
<div style="clear:both"></div>


'''18-k C-terminally trunucated small subunit of calpain'''
==See Also==
 
*[[Calpain 3D structures|Calpain 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The subunits in calpain and in the related penta-EF-hand (PEF) proteins are bound through contacts between the unpaired EF-hand 5 from each subunit. To study subunit binding further, a tetra-EF-hand 18 kDa N- and C-terminally truncated form of the calpain small subunit was prepared (18k). This protein does not combine with the calpain large subunit to form active calpain, but forms homodimers in solution, as shown by ultracentrifugation. The X-ray structure of the 18k protein in the presence of cadmium was solved to a resolution of 2.0 A. The structure of the monomer is almost identical to the known structure of the calpain small subunit, but the 18k protein forms an oligomer in the crystal by the use of two binding sites. One of these sites is an artefact arising from the C-terminal truncation, but the other is a naturally occurring site that is fully exposed to water in intact purified calpain. The characteristics of this site suggest that it may be important in binding other protein modulators involved in the regulation of calpain and of PEF proteins.
[[Category: Large Structures]]
 
==About this Structure==
1NP8 is a [[Single protein]] structure of sequence 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=1NP8 OCA].
 
==Reference==
A second binding site revealed by C-terminal truncation of calpain small subunit, a penta-EF-hand protein., Leinala EK, Arthur JS, Grochulski P, Davies PL, Elce JS, Jia Z, Proteins. 2003 Nov 15;53(3):649-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14579356 14579356]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Arthur JS]]
[[Category: Arthur, J S.]]
[[Category: Davies PL]]
[[Category: Davies, P L.]]
[[Category: Elce JS]]
[[Category: Elce, J S.]]
[[Category: Grochulski P]]
[[Category: Grochulski, P.]]
[[Category: Jia Z]]
[[Category: Jia, Z.]]
[[Category: Leinala EK]]
[[Category: Leinala, E K.]]
[[Category: dimer in solution]]
[[Category: oligomer in crystal]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:33:34 2008''

Latest revision as of 10:58, 14 February 2024

18-k C-terminally trunucated small subunit of calpain18-k C-terminally trunucated small subunit of calpain

Structural highlights

1np8 is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CPNS1_RAT Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1np8, resolution 2.00Å

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