NMR 对铜结合肽模型的铜金属伴侣蛋白的表征：对蛋氨酸作用的深入了解。
NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.
机构信息
Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel.
出版信息
Chem Commun (Camb). 2011 Jun 14;47(22):6407-9. doi: 10.1039/c1cc11600b. Epub 2011 May 9.
PMID:21552638
Abstract
The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ∼3.0 and ∼6.8 Cu(I) binds through one Cys and the Met rather than the two Cys residues, differently than at pH ∼8.5. This suggests a possible role of Met in metal transport.
摘要
该结构显示，在 pH 值约为 3.0 和 6.8 时，Cu（I）通过一个半胱氨酸和蛋氨酸而不是两个半胱氨酸残基结合，而不是在 pH 值约为 8.5 时的情况。这表明蛋氨酸在金属运输中可能具有作用。
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