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Crystal structure of the human odorant binding protein, OBP IIa
Author(s) -
Schiefner André,
Freier Regina,
Eichinger Andreas,
Skerra Arne
Publication year - 2015
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24797
Subject(s) - lipocalin , odorant binding protein , chemistry , monomer , biophysics , ligand (biochemistry) , protein structure , crystallography , molecule , plasma protein binding , binding site , barrel (horology) , biochemistry , biology , receptor , materials science , organic chemistry , composite material , gene , polymer
Human odorant‐binding protein, OBP IIa , is expressed by nasal epithelia to facilitate transport of hydrophobic odorant molecules across the aqueous mucus. Here, we report its crystallographic analysis at 2.6 Å resolution. OBP IIa is a monomeric protein that exhibits the classical lipocalin fold with a conserved eight‐stranded β‐barrel harboring a remarkably large hydrophobic pocket. Basic residues within the four loops that shape the entrance to this ligand‐binding site evoke a positive electrostatic potential. Human OBP IIa shows distinct features compared with other mammalian OBPs, including a potentially reactive Cys side chain within its pocket similar to human tear lipocalin. Proteins 2015; 83:1180–1184. © 2015 Wiley Periodicals, Inc.