1ztp

File:1ztp.gif

spinqualitylabelsall models 1ztp, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-ray structure of gene product from homo sapiens Hs.433573

OverviewOverview

The crystal structure of the human basophilic leukemia-expressed protein, (BLES03, p5326, Hs.433573) was determined by single-wavelength anomalous, diffraction and refined to an R factor of 18.8% (Rfree = 24.5%) at 2.5 A, resolution. BLES03 shows no detectable sequence similarity to any, functionally characterized proteins using state-of-the-art, sequence-comparison tools. The structure of BLES03 adopts a fold similar, to that of eukaryotic transcription initiation factor 4E (eIF4E), a, protein involved in the recognition of the cap structure of eukaryotic, mRNA. In addition to fold similarity, the electrostatic surface potentials, of BLES03 and eIF4E show a clear conservation of basic and acidic patches., In the crystal lattice, the acidic amino-terminal helices of BLES03, monomers are bound within the basic cavity of symmetry-related monomers in, a manner analogous to the binding of mRNA by eIF4E. Interestingly, the, gene locus encoding BLES03 is located between genes encoding the proteins, DRAP1 and FOSL1, both of which are involved in transcription initiation., It is hypothesized that BLES03 itself may be involved in a biochemical, process that requires recognition of nucleic acids.

About this StructureAbout this Structure

1ZTP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The structure at 2.5 A resolution of human basophilic leukemia-expressed protein BLES03., Bitto E, Bingman CA, Robinson H, Allard ST, Wesenberg GE, Phillips GN Jr, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Sep 1;61(Pt, 9):812-7. Epub 2005 Aug 31. PMID:16511166

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