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A model of the complex between human beta-microseminoprotein and CRISP-3 based on NMR data.

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Author

  • Houman Ghasriani
  • Per Fernlund
  • Lene Udby
  • Torbjörn Drakenberg

Summary, in English

beta-Microseminoprotein (MSP), a 10kDa seminal plasma protein, forms a tight complex with cysteine-rich secretory protein 3 (CRISP-3) from granulocytes. The 3D structure of human MSP has been determined but there is as yet no 3D structure for CRISP-3. We have now studied the complex between human MSP and CRISP-3 with multidimensional NMR. (15)N-HSQC spectra show substantial differences between free and complexed hMSP. Using several 3D-NMR spectra of triply labeled hMSP in complex with a recombinant N-terminal domain of CRISP-3, most of the backbone of hMSP could be assigned. The data show that only one side of hMSP, comprising beta-strands 1, 4, 5, and 8 are affected by the complex formation, indicating that beta-strands 1 and 8 form the main binding surface. Based on this we present a tentative structure for the hMSP-CRISP-3 complex using the known crystal structure of triflin as a model of CRISP-3.

Publishing year

2009

Language

English

Pages

235-239

Publication/Series

Biochemical and Biophysical Research Communications

Volume

378

Issue

2

Document type

Journal article

Publisher

Elsevier

Topic

  • Biological Sciences

Status

Published

Research group

  • Clinical Chemistry, Malmö

ISBN/ISSN/Other

  • ISSN: 1090-2104