Crystal structure of human platelet-derived growth factor BB.
The crystal structure of the homodimeric BB isoform of human recombinant platelet-derived growth factor (PDGF-BB) has been determined by X-ray analysis to 3.0 A resolution. The polypeptide chain is folded into two highly twisted antiparallel pairs of beta-strands and contains an unusual knotted arrangement of three intramolecular disulfide bonds. Dimerization leads to the clustering of three surface loops at each end of the elongated dimer, which most probably form the receptor recognition sites.
Oefner
C
C
Department of Pharmaceutical Research--New Technologies, F. Hoffmann-La Roche Ltd., Basel, Switzerland.
D'Arcy
A
A
Winkler
F K
FK
Eggimann
B
B
Hosang
M
M
D000595:Amino Acid Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D004220:Disulfides / Q000032:analysis; D006801:Humans; D046911:Macromolecular Substances; D008958:Models, Molecular; D010982:Platelet-Derived Growth Factor / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000235:genetics; D017384:Sequence Deletion; D014961:X-Ray Diffraction / Q000379:methods
D004220:Disulfides; D046911:Macromolecular Substances; D010982:Platelet-Derived Growth Factor; D011994:Recombinant Proteins