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Binding domains and epitopes in platelet-derived growth factor.

Authors
  • Vogel, S
  • Hoppe, J
Type
Published Article
Journal
Biochemistry
Publication Date
Apr 04, 1989
Volume
28
Issue
7
Pages
2961–2966
Identifiers
PMID: 2472833
Source
Medline
License
Unknown

Abstract

Trypsin treatment of recombinant PDGF-BB from Escherichia coli leads to the liberation of a small carboxy-terminal fragment and two internal segments without dissociating the molecule. The remaining core of 21 kDa retained a considerable binding affinity of 8.4 nM. By use of various peptide fragments obtained from monomeric recombinant PDGF-B, a receptor binding domain was assigned to one of these internal trypsin-sensitive segments. This segment is enriched in charged residues, suggesting mainly hydrophilic interactions with the receptor. Circular dichroism measurements of recombinant PDGF-BB showed a high content of random structure and only a small percentage (less than 10%) of alpha-helical structures. This structure was very rigid since the addition of 70% trifluoroethanol or 1% SDS did not change the circular dichroism spectrum. On the basis of these results, a tentative structure was generated by computer modeling.

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