1ak8
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NMR SOLUTION STRUCTURE OF CERIUM-LOADED CALMODULIN AMINO-TERMINAL DOMAIN (CE2-TR1C), 23 STRUCTURES
OverviewOverview
The solution structure of the dicerium(III) complex of the N-terminal, domain of calmodulin (Ce2-TR1C hereafter) has been solved employing, paramagnetic T1 relaxation enhancements and pseudocontact shifts, introduced by the Ce3+ ions, together with conventional NOE constraints., The use of pseudocontact shift constraints constitutes the first attempt, to locate metal ions within a protein structure by NMR. Like calcium(II), paramagnetic cerium(III) has been found to bind to the two metal binding, sites of the TR1C fragment of calmodulin in a cooperative manner. Due to, the presence of pseudocontact interactions between the Ce3+ ions and, protons of the 76-residue protein, the 1H NMR spectra of the complex show, resonances shifted between +22 and -9 ppm. Eighty percent of its proton, ... [(full description)]
About this StructureAbout this Structure
1AK8 is a [Single protein] structure of sequence from [Bos taurus] with CE as [ligand]. Structure known Active Sites: EF1 and EF2. Full crystallographic information is available from [OCA].
ReferenceReference
Solution structure of the paramagnetic complex of the N-terminal domain of calmodulin with two Ce3+ ions by 1H NMR., Bentrop D, Bertini I, Cremonini MA, Forsen S, Luchinat C, Malmendal A, Biochemistry. 1997 Sep 30;36(39):11605-18. PMID:9305950
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