The compact domain conformation of human Glu-plasminogen in solution

C P Ponting, S K Holland, S A Cederholm-Williams, J M Marshall, A J Brown, G Spraggon, C C Blake

Research output: Contribution to journalArticlepeer-review


A complete understanding of the accelerating mechanisms of plasminogen activation and fibrinolysis necessarily requires structural information on the conformational forms of plasminogen. Given the absence of high-resolution structural data on plasminogen the use of lower resolution approaches has been adopted. Two such approaches have previously indicated a compact conformation of Glu-plasminogen (Tranqui, L., Prandini, M., and Chapel, A. (1979) Biol. Cellulaire, 34, 39-42; Bányai, L. and Patthy, L. (1985) Biochim. Biophys. Acta, 832, 224-227) whereas a third has suggested a fairly extended conformation (Mangel, W., Lin, B. and Ramakrishnan, V. (1990) Science, 248, 69-73). Native Glu-plasminogen has been investigated using small-angle X-ray scattering (SAXS) experiments. It is concluded that this molecule in solution is compact (radius of gyration, RG 3.05 +/- 0.02 nm and maximum intramolecular distance, Im 9.1 +/- 0.3 nm) and that the data are consistent with the right-handed spiral structure observed using electron microscopy by Tranqui et al. (1979). A spiral structure of native plasminogen would have important implications for the conformational response of plasminogen to fibrin and concomitant stimulation of plasminogen activation.

Original languageEnglish
Pages (from-to)155-61
Number of pages7
JournalBBA - Bioenergetics
Issue number2
Publication statusPublished - 23 Sep 1992


  • Computer Simulation
  • Humans
  • Models, Molecular
  • Plasminogen
  • Protein Conformation
  • Scattering, Radiation
  • Solutions


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