also see
http://biologicalchem.med.utah.edu/bock/bock.html
My lab studies the anticoagulant protein antithrombin III (ATIII). Primary goals of our work are to understand the structural basis of ATIII heparin cofactor activity and the physiological expression of ATIII anticoagulant activity on and in the vessel wall. We are also employing our knowledge of antithrombin III and serpin structure/function relationships to design and develop clinically useful, neutrophil-resistant serpins for use in sepsis and other inflammatory pathologies.
Turk, B., Brieditis, I., Bock, S.C., Olson, S.T., and Bjork, I.
1997.
The oligosaccharide Side Chain on Asn-135 of alpha-Antithrombin, Absent
in
beta-Antithrombin, Decreases the Heparin Affinity of the Inhibitor by
Affecting the Heparin-Induced Conformational Change. Biochemistry,
36:
6682-6691
Ersdal-Badju, E., Lu, A., Zuo, Y., Picard, V. and Bock, S.C. 1997.
Identification of the Antithrombin III Heparin Binding Site. J. Biol.
Chem., 272: 19393-19400
Picard, V., and Bock, S.C. 1996. Rapid and efficient one-tube
PCR-based
mutagenesis method. In Methods in Molecular Biology: PCR Protocols
B.A. White, ed. Humana Press, Totowa, NJ. pp.183-186
Ersdal-Badju, E., Lu, A., Peng, X., Picard, V., Zendehrouh, P., Turk,
B.,
Bjrk, I., Olson, S.T., and Bock, S.C. 1995. Elimination of glycosylation
heterogeneity affecting heparin affinity of recombinant human antithrombin
III by expression of a beta-like variant in baculovirus-infected insect
cells. Biochem. J., 310: 323-330
Picard, V., Ersdal-Badju, E., and Bock, S.C. 1995. Partial
glycosylation
of antithrombin III asparagine-135 is caused by the serine in the
third
position of its N-glycosylation consensus sequence and responsible for the
production of the beta-ATIII isoform with enhanced heparin affinity.
Biochemistry, 34: 8433-8440