Crystal structure of the human odorant binding protein, OBPIIa.
Proteins
; 83(6): 1180-4, 2015 Jun.
Article
em En
| MEDLINE
| ID: mdl-25810031
ABSTRACT
Human odorant-binding protein, OBPIIa , 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. OBPIIa is a monomeric protein that exhibits the classical lipocalin fold with a conserved eight-stranded ß-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 OBPIIa shows distinct features compared with other mammalian OBPs, including a potentially reactive Cys side chain within its pocket similar to human tear lipocalin.
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MEDLINE
Assunto principal:
Lipocalinas
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article