A model of the complex between human {beta}-microseminoprotein and CRISP-3 based on NMR data
- Department of Biophysical Chemistry, Lund University, Po Box 124, 22100 Lund (Sweden)
- Department of Laboratory Medicine, Lund University, University Hospital MAS, Malmoe (Sweden)
- Granulocyte Research Laboratory, Department of Hematology, Rigshospitalet, Copenhagen University Hospital (Denmark)
{beta}-Microseminoprotein (MSP), a 10 kDa 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. {sup 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.
- OSTI ID:
- 21255827
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 378, Issue 2; Other Information: DOI: 10.1016/j.bbrc.2008.11.040; PII: S0006-291X(08)02215-8; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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