Proximity of the catalytic region and the kringle 2 domain in the closed conformer of plasminogen

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Abstract

Introduction of a single intramolecular cross-link with 1,5-difluoro-2,4-dinitrobenzene into Glu-plasminogen freezes the molecule in its closed conformational state (Bányai, L. and Patthy, L. (1984) J. Biol. Chem. 259, 6466-6471). Here we show that the cross-link connects Lys-203 of the kringle 2 domain and Tyr-671 of the catalytic domain, indicating that these regions are in close proximity in the closed conformer of Glu-plasminogen. Comparison of the parameters of the urokinase-catalysed activation of native and cross-linked Glu-plasminogen species indicates that cross-linking of kringle 2 and the catalytic region interferes with the productive binding of urokinase to plasminogen.

Original languageEnglish
Pages (from-to)224-227
Number of pages4
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume832
Issue number2
DOIs
Publication statusPublished - Nov 29 1985

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Keywords

  • (Human)
  • Chemical cross-linking
  • Kringle 2 domain
  • Plasminogen
  • Urokinase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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