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Bächinger Lab Research
Interest:
Collagen structure, stability and folding.
We are trying to decipher the basic principles which govern
collagen folding and stability. For this purpose we need to know
detailed atomic structures and biophysical properties of different
collagen domains: triple helix, cystine knots and specific
trimerization domains. Chain selection, association, specific
staggering of triple helix, folding and stability of collagens are
key questions of our research.
BIOGRAPHICAL SKETCH
Name:
Sergei Boudko
Role on Project:
Postdoc
Institution & Location
Degree
Year(s) Field of Study
Moscow
Institute of Physics and Technology
Diploma 1999 Mathematics & Physics
University of Basel, Switzerland Ph.D. 2003 Biophysics
Research and/or
Professional Experience:
2006-Present Postdoctoral Fellow with Dr. Hans Peter Bächinger,
Shriners Hospitals for Children, OHSU, Portland, Oregon
2004-2006 Postdoctoral Researcher with Professor Michael G. Rossmann,
Department of Biological Sciences, Purdue University, West
Lafayette, Indiana
2003-2004 Postdoctoral Fellow with Professor PD Juergen Engel,
Department of Biophysical Chemistry, Biozentrum, University of
Basel, Basel, Switzerland
Publications:
1. Boudko SP, Sasaki T,
Engel J, Lerch TF, Nix J, Chapman MS, Bächinger HP. Crystal
STructure of Human Collagen XVIII Trimerization Domain: A NOvel
Collagen Trimerization Fold. J MOl Biol. 2009 Jul 23
2. Okuyama K, Bächinger HP, Mizuno K, Boudko
S, Engel J, Berisio R, Vitagliano L, Re: Microfibrillar structure of
type I collagen in situ. Aceta Crystallogr D Biol Crystallogr. 2009
Sep;65(Pt 9):1007-8
3. Boudko SP, Engel J, Bächinger HP.
Trimerization and triple helix stabilization of the collagen XIX NC2
domain. J Biol Chem. 2008
Dec 5;283(49):34345-51
4. Boudko SP, Engel J, Okuyama K, Mizuno K, Bachinger HP,
Schumacher MA.Crystal structure of human type III collagen
G991-G1032 cystine knot containing peptide shows both 7/2 and 10/3
triple helical symmetries. J Biol Chem.
2008 Nov 21;283(47):32580-9
5. Boudko SP, Kuhn RJ, Rossmann MG.
The coiled-coil domain structure of the Sin Nombre virus
nucleocapsid protein. J Mol Biol. 2007 Mar
9; 366(5):1538-44
6. Bachmann A, Kiefhaber T, Boudko S, Engel J, Bächinger HP.
Collagen triple-helix formation in all-trans chains proceeds
by a nucleation/growth mechanism with a purely entropic barrier.
Proc Natl Acad Sci U S A. 2005; 102(39):13897-902.
7. Boudko SP, Strelkov SV, Engel J, Stetefeld J.
Design and crystal structure of bacteriophage T4
mini-fibritin NCCF. J Mol Biol. 2004;
339(4):927-35.
8. Boudko SP, Engel J. Structure
formation in the C terminus of type III collagen guides disulfide
cross-linking. J Mol Biol. 2004;
335(5):1289-97.
9. Stetefeld J, Frank S, Jenny M, Schulthess T, Kammerer RA,
Boudko S, Landwehr R, Okuyama K, Engel J.
Collagen stabilization at atomic level: crystal structure of
designed (GlyProPro)10foldon. Structure.
2003; 11(3):339-46.
10. Frank S, Boudko S, Mizuno K, Schulthess T, Engel J,
Bächinger HP.Collagen triple helix formation can be nucleated at
either end.J Biol Chem. 2003; 278(10):7747-50.
11. Boudko S, Frank S, Kammerer RA, Stetefeld J, Schulthess T,
Landwehr R, Lustig A, Bächinger HP, Engel J.Nucleation and
propagation of the collagen triple helix in single-chain and
trimerized peptides: transition from third to first order kinetics.J
Mol Biol. 2002; 317(3):459-70.
12. Boudko SP, Londer YY, Letarov AV, Sernova NV, Engel J,
Mesyanzhinov VV.Domain organization, folding and stability of
bacteriophage T4 fibritin, a segmented coiled-coil protein.Eur J
Biochem. 2002; 269(3):833-41.
13. Shneider MM, Boudko SP, Lustig A, Mesyanzhinov VV.Properties
of bacteriophage T4 baseplate protein encoded by gene 8.Biochemistry
(Mosc). 2001; 66(6):693-7.
14. Letarov AV, Londer YY, Boudko SP, Mesyanzhinov VV.The
carboxy-terminal domain initiates trimerization of bacteriophage T4
fibritin.Biochemistry (Mosc). 1999; 64(7):817-23.
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Ph.D.
