Functional linkage between the S1 site, sodium site, and the calcium site in 
the protease domain of human activated protein C (APC): Evidence that sodium 
coordinates to four carbonyl groups from two separate loops of APC.

Bajaj, S. P.; Underwood, M. C.; Schmidt, A. E.; Padmanabhan, K.; Bode, W.; Mather, T.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Functional linkage between the S1 site, sodium site, and the calcium site in the protease domain of human activated protein C (APC): Evidence that sodium coordinates to four carbonyl groups from two separate loops of APC.

MPS-Authors

/persons/resource/persons77772

Bode, W.
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Bajaj, S. P., Underwood, M. C., Schmidt, A. E., Padmanabhan, K., Bode, W., & Mather, T. (2001). Functional linkage between the S1 site, sodium site, and the calcium site in the protease domain of human activated protein C (APC): Evidence that sodium coordinates to four carbonyl groups from two separate loops of APC. Blood, 98(11), 199.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-7104-9

Abstract

There is no abstract available