A model of the complex between human beta-microseminoprotein and CRISP-3 based on NMR data
Research output: Contribution to journal › Journal article › Research › peer-review
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 |
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Journal | Biochemical and Biophysical Research Communications |
Volume | 378 |
Issue number | 2 |
Pages (from-to) | 235-9 |
Number of pages | 4 |
ISSN | 0006-291X |
DOIs | |
Publication status | Published - 2008 |
Bibliographical note
Keywords: Amino Acid Sequence; Crystallography; Humans; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Prostatic Secretory Proteins; Protein Structure, Secondary; Salivary Proteins and Peptides; Seminal Plasma Proteins
ID: 20195034