Molecular and crystal properties of Bos d 2, an allergenic protein of the lipocalin family.
The relationship between the molecular structure of allergenic proteins and the allergenic determinants is one of the central issues in allergology. We report here that the natural preparation of Bos d 2, a mammalian lipocalin allergen, comprises three molecular variant proteins of 17,829, 17,781, and 17,800 Da. When cDNA of Bos d 2 (Genome Sequence Data Base No. L42867) was recloned and expressed in Pichia pastoris, two proteins were produced. One of the proteins (17,831 Da) and the proteins in the natural preparation had pyroglutamate as the N-terminal residue; in the other (17,849 Da) the N-terminal residue was glutamine. Recombinant Bos d 2 protein was crystallized and the native data set was collected at 1.8 A resolution.
Rautiainen
J
J
Department of Clinical Microbiology, University of Kuopio, Finland.
Auriola
S
S
Rouvinen
J
J
Kauppinen
J
J
Zeiler
T
T
Novikov
D
D
Virtanen
T
T
Mäntyjärvi
R A
RA
D000485:Allergens / Q000737:chemistry*; D000818:Animals; D052179:Antigens, Plant; D002352:Carrier Proteins / Q000737:chemistry*; D002417:Cattle; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D013058:Mass Spectrometry; D010675:Pheromones / Q000737:chemistry; D010843:Pichia / Q000235:genetics; D011761:Pyrrolidonecarboxylic Acid / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D013545:Sweat Glands / Q000737:chemistry
D000485:Allergens; D052179:Antigens, Plant; C113339:Bos d 2 allergen; D002352:Carrier Proteins; D010675:Pheromones; D011994:Recombinant Proteins; D011761:Pyrrolidonecarboxylic Acid