A model of the complex between human beta-microseminoprotein and CRISP-3 based on NMR data.
(2009) In Biochemical and Biophysical Research Communications 378(2). p.235-239- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1271181
- author
- Ghasriani, Houman LU ; Fernlund, Per LU ; Udby, Lene and Drakenberg, Torbjörn LU
- organization
- publishing date
- 2009
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochemical and Biophysical Research Communications
- volume
- 378
- issue
- 2
- pages
- 235 - 239
- publisher
- Elsevier
- external identifiers
-
- wos:000262063100018
- pmid:19026612
- scopus:57049165364
- ISSN
- 1090-2104
- DOI
- 10.1016/j.bbrc.2008.11.040
- language
- English
- LU publication?
- yes
- id
- 2c7ef51c-74c5-494b-a717-16bc0e810cb0 (old id 1271181)
- date added to LUP
- 2016-04-01 14:11:56
- date last changed
- 2022-03-14 04:36:00
@article{2c7ef51c-74c5-494b-a717-16bc0e810cb0, 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.}}, author = {{Ghasriani, Houman and Fernlund, Per and Udby, Lene and Drakenberg, Torbjörn}}, issn = {{1090-2104}}, language = {{eng}}, number = {{2}}, pages = {{235--239}}, publisher = {{Elsevier}}, series = {{Biochemical and Biophysical Research Communications}}, title = {{A model of the complex between human beta-microseminoprotein and CRISP-3 based on NMR data.}}, url = {{http://dx.doi.org/10.1016/j.bbrc.2008.11.040}}, doi = {{10.1016/j.bbrc.2008.11.040}}, volume = {{378}}, year = {{2009}}, }