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

Houman Ghasriani, Per Fernlund, Lene Udby, Torbjörn Drakenberg

Research output: Contribution to journalArticlepeer-review

Abstract

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.
Original languageEnglish
Pages (from-to)235-239
JournalBiochemical and Biophysical Research Communications
Volume378
Issue number2
DOIs
Publication statusPublished - 2009

Subject classification (UKÄ)

  • Biological Sciences

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