Sequential assignment of 1H, 15N, 13C resonances and secondary structure of human calmodulin-like protein determined by NMR spectroscopy

Hong Qian, Michael S. Rogers, Jürgen Schleucher, Ulf Edlund, Emanuel E. Strehler, Ingmar Sethson

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


Human calmodulin-like protein (CLP) is closely related to vertebrate calmodulin, yet its unique cell specific expression pattern, overlapping but divergent biochemical properties, and specific target proteins suggest that it is not an isoform of calmodulin. To gain insight into the structural differences that may underlie the difference target specificities and biochemical properties of CLP when compared to calmodulin, we determined the sequential backbone assignment and associated secondary structure of 144 out of the 148 residues of Ca2+-CLP by using multinuclear multidimensional NMR spectroscopy. Despite a very high overall degree of structural similarity between CLP and calmodulin, a number of significant differences were found mainly in the length of α-helices and in the central nonhelical flexible region. Interestingly, the regions of greatest primary sequence divergence between CLP and calmodulin in helices III and VIII displayed only minor secondary structure differences. The data suggest that the distinct differences in target specificity and biochemical properties of CLP and calmodulin result from the sum of several minor structural and side-chain changes spread over multiple domains in these proteins.

Original languageEnglish (US)
Pages (from-to)2421-2430
Number of pages10
JournalProtein Science
Issue number11
StatePublished - Nov 1998


  • Calmodulin-like protein
  • NMR
  • Secondary structural analysis
  • Sequential assignment

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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