Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum

Shuren Wang, William R. Trumble, Hong Liao, Carla R. Wesson, A. Keith Dunker, Chul Hee Kang

Research output: Contribution to journalArticle

188 Scopus citations


Caisequestrin, the major Ca2+ storage protein of muscle, coordinately binds and releases 40-50 Ca2+ ions per molecule for each contraction- relaxation cycle by an uncertain mechanism. We have determined the structure o rabbit skeletal muscle calsequestrin. Three very negative thioredoxin-like domains surround a hydrophilic center. Each monomer makes two extensive dimerization contacts, both of which involve the approach of many negative groups. This structure suggests a mechanism by which calsequestrin may achieve high capacity Ca2+ binding. The suggested mechanism involves Ca2+-induced collapse of the three domains and polymerization of calsequestrin monomers arising from three factors: N-terminal arm exchange, helix-helix contacts and Ca2+ cross bridges. This proposed structure-based mechanism accounts for the observed coupling of high capacity Ca2+ binding with protein precipitation.

Original languageEnglish (US)
Pages (from-to)476-483
Number of pages8
JournalNature Structural Biology
Issue number6
StatePublished - Jun 1 1998
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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