The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode 
for a linear epitope of the SKIP protein.

Stegmann, C.; Lührmann, R.; Wahl, M. C.

doi:10.1371/journal.pone.0010013

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein.

MPS-Authors

/persons/resource/persons15864

Stegmann, C.
Research Group of X-Ray Crystallography, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15470

Lührmann, R.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15983

Wahl, M. C.
Research Group of X-Ray Crystallography, MPI for biophysical chemistry, Max Planck Society;

External Resource

http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0010013
(Publisher version)

Fulltext (restricted access)

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

Fulltext (public)

475986.pdf
(Publisher version), 0B

Supplementary Material (public)

There is no public supplementary material available

Citation

Stegmann, C., Lührmann, R., & Wahl, M. C. (2010). The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein. PLoS ONE, 5: e10013. doi:10.1371/journal.pone.0010013.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-D5E3-F

Abstract

There is no abstract available