| Autor: |
Ohki, Shin-ya, Miura, Kazunori, Saito, Moyoko, Nakashima, Ken-ichi, Maekawa, Hironobu, Yazawa, Michio, Tsuda, Sakae, Hikichi, Kunio |
| Předmět: |
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| Zdroj: |
Journal of Biochemistry; 1996, Vol. 119 Issue 6, p1045-1055, 11p |
| Abstrakt: |
Using two- and three-dimensional NMR techniques, 1H and main-chain 15N resonances of the N-terminal half domain of yeast calmodulin (YCMO-N) in the presence of Mg2+ and Ca2+ (Mg2+- and Ca2+-forms) were assigned. The secondary structures of YCMO-N in both forms were determined. The NOESY and 15N-edited NOESY spectra of YCMO-N in each form indicate that there is a hydrophobic core and that two Ca2+-binding loops are connected by a short antiparallel β-sheet. There are four helices (A, B, C, and D named from the N-terminus) for YCMO-N in the Mg2+-form. The B-helix is, however, not formed in the Ca2+-form. The Ca2+-binding of YCMO-N was monitored by (1H,15N)-HSQC at various Ca2+ concentrations. The observed spectral changes as a function of Ca2+-concentration can not readily be grouped into a small number of classes; each residue shows individual spectral change. There is no apparent relationship between the spectral change and the type or location of the amino acid concerned. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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