1np8: Difference between revisions

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[[Image:1np8.jpg|left|200px]]<br /><applet load="1np8" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1np8.jpg|left|200px]]
caption="1np8, resolution 2.00&Aring;" />
 
'''18-k C-terminally trunucated small subunit of calpain'''<br />
{{Structure
|PDB= 1np8 |SIZE=350|CAPTION= <scene name='initialview01'>1np8</scene>, resolution 2.00&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene>
|ACTIVITY=
|GENE= CAPNS1 OR CAPN4 OR CSS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
}}
 
'''18-k C-terminally trunucated small subunit of calpain'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1NP8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NP8 OCA].  
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==
==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=14579356 14579356]
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: Single protein]]
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[[Category: oligomer in crystal]]
[[Category: oligomer in crystal]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:32 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:59:52 2008''

Revision as of 13:59, 20 March 2008

File:1np8.jpg


PDB ID 1np8

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands:
Gene: CAPNS1 OR CAPN4 OR CSS1 (Rattus norvegicus)
Coordinates: save as pdb, mmCIF, xml



18-k C-terminally trunucated small subunit of calpain


OverviewOverview

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.

About this StructureAbout this Structure

1NP8 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

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:14579356

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