This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1sji

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sji.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1sji.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sji| PDB=1sji | SCENE= }}
{{STRUCTURE_1sji| PDB=1sji | SCENE= }}
-
'''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==
+
<!--
-
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
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14871888 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14871888}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Glycoprotein]]
[[Category: Glycoprotein]]
[[Category: Muscle protein]]
[[Category: Muscle protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:46:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:33:08 2008''

Revision as of 07:33, 28 July 2008

Image:1sji.png

Template:STRUCTURE 1sji

Comparing 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 Structure

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

Reference

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

Page seeded by OCA on Mon Jul 28 10:33:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sji"
Personal tools