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Article

Modeling, substrate docking, and mutational analysis identify residues essential for the function and specificity of a eukaryotic purine-cytosine NCS1 transporter.

The Journal of biological chemistry - 26 Oct 2012

Krypotou Emilia, Kosti Vasiliki, Amillis Sotiris, Myrianthopoulos Vassilios, Mikros Emmanuel, Diallinas George

Abstract excerpt

The recent elucidation of crystal structures of a bacterial member of the NCS1 family, the Mhp1 benzyl-hydantoin permease from Microbacterium liquefaciens, allowed us to construct and validate a three-dimensional model of the Aspergillus nidulans purine-cytosine/H(+) FcyB symporter. The model consists of 12 transmembrane α-helical, segments (TMSs) and cytoplasmic N- and C-tails. A distinct core of 10 TMSs is made...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 22969088
DOI: 10.1074/jbc.M112.400382
PMCID: PMC3481282

Genes

NCS1

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