1sji: Difference between revisions

Revision as of 10:33, 28 July 2008

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File:1sji.png

Template:STRUCTURE 1sji

Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerizationComparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization

Template:ABSTRACT PUBMED 14871888

About this StructureAbout this Structure

1SJI is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.

ReferenceReference

Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization., Park H, Park IY, Kim E, Youn B, Fields K, Dunker AK, Kang C, J Biol Chem. 2004 Apr 23;279(17):18026-33. Epub 2004 Feb 10. PMID:14871888

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-'''Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization'''
+===Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization===
-==Overview==
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-Calsequestrin, the major calcium storage protein of both cardiac and skeletal muscle, binds and releases large numbers of Ca(2+) ions for each contraction and relaxation cycle. Here we show that two crystal structures for skeletal and cardiac calsequestrin are nearly superimposable not only for their subunits but also their front-to-front-type dimers. Ca(2+) binding curves were measured using atomic absorption spectroscopy. This method enables highly accurate measurements even for Ca(2+) bound to polymerized protein. The binding curves for both skeletal and cardiac calsequestrin were complex, with binding increases that correlated with protein dimerization, tetramerization, and oligomerization. The Ca(2+) binding capacities of skeletal and cardiac calsequestrin are directly compared for the first time, with approximately 80 Ca(2+) ions bound per skeletal calsequestrin and approximately 60 Ca(2+) ions per cardiac calsequestrin, as compared with net charges for these molecules of -80 and -69, respectively. Deleting the negatively charged and disordered C-terminal 27 amino acids of cardiac calsequestrin results in a 50% reduction of its calcium binding capacity and a loss of Ca(2+)-dependent tetramer formation. Based on the crystal structures of rabbit skeletal muscle calsequestrin and canine cardiac calsequestrin, Ca(2+) binding capacity data, and previous light-scattering data, a mechanism of Ca(2+) binding coupled with polymerization is proposed.
+The line below this paragraph, {{ABSTRACT_PUBMED_14871888}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_14871888}}
 ==About this Structure==
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 [[Category: Glycoprotein]]
 [[Category: Muscle protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:46:55 2008''
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