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The structure at 2.5 Å resolution of human basophilic leukemia-expressed protein BLES03

Acta Cryst. (2005). F61, 812–817

The crystal structure of the 27.5 kDa human basophilic leukemia-expressed protein (BLES03, p5326, Hs.433573) was determined at 2.5 Å resolution. Despite having an undetectable sequence relationship, the structure adopts a fold similar to that of eukaryotic initiation factor 4E with minor variations. The observed similarity extends beyond the shared fold and encompasses the conservation of both the electrostatic surface potential and the location of a binding cavity. It is hypothesized that BLES03 itself may be involved in a biochemical process that requires recognition of nucleic acids.
Eduard Bitto, Craig A. Bingman, Howard Robinson, Simon T. M. Allard, Gary E. Wesenberg and George N. Phillips Jr