Long-range effects on calcium binding and conformational change in the N-domain of calmodulin.
In: Biochemistry, Jg. 40 (2001-10-23), Heft 42, S. 12719-26
academicJournal
Zugriff:
Proteins within the EF-hand protein family exhibit different conformational responses to Ca(2+) binding. Calmodulin and other members of the EF-hand protein family undergo major changes in conformation upon binding Ca(2+). However, some EF-hand proteins, such as calbindin D9k (Clb), bind Ca(2+) without a significant change in conformation. Here, we investigate the effects of replacement of a leucine at position 39 of the N-terminal domain of calmodulin (N-Cam) with a phenylalanine derived from Clb. This variant is studied alone and in the context of other mutations that affect the conformational properties of N-Cam. Strikingly, the introduction of Phe39, which is distant from the calcium binding sites, leads to a significant enhancement of Ca(2+) binding affinity, even in the context of other mutations which trap the protein in the closed form. The results yield novel insights into the evolution of EF-hand proteins as calcium sensors versus calcium buffers.
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Long-range effects on calcium binding and conformational change in the N-domain of calmodulin.
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Autor/in / Beteiligte Person: | Ababou, A ; Shenvi, RA ; Desjarlais, JR |
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Zeitschrift: | Biochemistry, Jg. 40 (2001-10-23), Heft 42, S. 12719-26 |
Veröffentlichung: | Washington, American Chemical Society., 2001 |
Medientyp: | academicJournal |
ISSN: | 0006-2960 (print) |
DOI: | 10.1021/bi010405b |
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