Atomic resolution view into the structure–function relationships of the human myelin peripheral membrane protein P2

Ruskamo, S.; Yadav, R.P.; Sharma, S.; Lehtimäki, M.; Laulumaa, S.; Aggarwal, S.; Simons, M.; Bürck, J.; Ulrich, A.S.; Juffer, A.H.; Kursula, I.; Kursula, P.

doi:10.1107/S1399004713027910

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 2
Anisotropy and dynamics in human P2. (a) Alternative conformations in residues interacting with the fatty acid in the binding cavity. (b) Main-chain mean anisotropy along the human P2 sequence. A fully isotropic atom has an anisotropy of 1.0. (c) Atomistic simulation of apo (black) and liganded (red) P2 based on a 30 ns trajectory. The difference between the apo and liganded simulations is shown in green.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 1| December 2014| Pages 165-176

doi:10.1107/S1399004713027910

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