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Content archived on 2024-04-16

Structural basis for Ca2+-transport by the sarcoplasmic Ca2+-pump protein

Objective



The proposal aims at a concerted effort to explore the molecular mechanism of sarcoplasmic reticulum Ca2+-ATPase, a representative of the P type cation transporting ATPases. Ca2+-ATPase structure will be studied by the use of proteolytic dissection, immunolocalization, and chemical modification experiments to define the location of membrane buried and exposed segments of the polypeptide chain and Ca2+ transport sites. Molecular biology tools will be used to develop a yeast system to express relatively large amounts of Ca2+-ATPase mutants to pinpoint amino acid residues involved in Ca2+-binding. Functionally oriented studies will include examination of Ca2+-binding and -release by rapid kinetic experiments. In addition domain organization and proximity-relationships of strategic sites (ATP, phosphorylation, and Ca2+ binding) will be studied by fluorescence experiments, reaction with site-specific antibodies, and differential scanning calorimetry. The results obtained will be combined in an attempt to produce a functionally relevant structural model for Ca2+-
ATPase.

Topic(s)

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Call for proposal

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Coordinator

Århus Universitet
EU contribution
No data
Address
185,Ole Worms Allé
8000 Århus C
Denmark

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Total cost
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Participants (4)