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 language | English |
|---|---|
| Pages (from-to) | 235-239 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 378 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2009 |
Subject classification (UKÄ)
- Biological Sciences
Fingerprint
Dive into the research topics of 'A model of the complex between human beta-microseminoprotein and CRISP-3 based on NMR data.'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver