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Article

Mutation of Ser-50 and Cys-66 in Snapin modulates protein structure and stability.

Biochemistry - 24 Apr 2012

Navarro Aaron, Encinar José A, López-Méndez Blanca, Aguado-Llera David, Prieto Jesús, Gómez Javier, Martínez-Cruz Luís Alfonso, Millet Oscar, González-Ros José Manuel, Fernández-Ballester Gregorio, Neira José L, Ferrer-Montiel Antonio

Abstract excerpt

Snapin is a 15 kDa protein present in neuronal and non-neuronal cells that has been implicated in the regulation of exocytosis and endocytosis. Protein kinase A (PKA) phosphorylates Snapin at Ser-50, modulating its function. Likewise, mutation of Cys-66, which mediates protein dimerization, impairs its cellular activity. Here, we have investigated the impact of mutating these two positions on protein...

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Cysteine
Protein Conformation
Protein Stability
Protein Structure, Secondary
Serine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Spectroscopy, Fourier Transform Infrared

Vesicular Transport Proteins

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PMID: 22471585
DOI: 10.1021/bi201574t

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