Crystallization and functional analysis of a soluble deglycosylated form of the human costimulatory molecule B7-1.
Acta Crystallogr D Biol Crystallogr
; 57(Pt 4): 605-8, 2001 Apr.
Article
em En
| MEDLINE
| ID: mdl-11264596
ABSTRACT
The interactions of B7-1 with CD28 and CTLA-4 modulate the course of human immune responses, making B7-1 an important target for developing structure-based therapeutics. B7-1 is, however, one of the most heavily glycosylated proteins found at the leukocyte cell surface, complicating the structural analysis of this molecule. Methods for the production, crystallization and selenomethionine labelling of a soluble deglycosylated form of this molecule are described. The protein readily forms both tetragonal plate and bipyramidal crystals belonging to space groups I4(1)22, with unit-cell parameters a = b = 56.9, c = 298.7 A, and P4(1)22 (or P4(3)22), with unit-cell parameters a = b = 89.0, c = 261.9 A, respectively. The I4(1)22 and primitive crystal forms diffract to 2.7 and 3.5 A, respectively. Surface plasmon resonance-based assays indicate that the ligand-binding properties of sB7-1 are unaffected by deglycosylation. Since none of the methods relied on any special structural properties of sB7-1, it is proposed that this novel combination of procedures could in principle be adapted to the systematic analysis of many other glycoproteins of structural or functional interest.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Antígeno B7-1
/
Imunoconjugados
Limite:
Humans
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Ano de publicação:
2001
Tipo de documento:
Article
País de afiliação:
Reino Unido