1np8: Difference between revisions

Revision as of 15:06, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1np8.png

Template:STRUCTURE 1np8

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

Template:ABSTRACT PUBMED 14579356

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''18-k C-terminally trunucated small subunit of calpain'''
+===18-k C-terminally trunucated small subunit of calpain===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14579356}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14579356 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14579356}}
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 [[Category: Dimer in solution]]
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