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 6
Membrane binding by P2. (a) Binding of P2 to DMPA monolayers in SPR. (b) A raw SPR sensorgram with injections in rapid succession: 1.5 µM BSA followed by 50, 100, 200, 500, 1000 and 2000 nM P2. (c) Small-angle X-ray diffraction of P2 and MBP mixed with DMPC/DMPG vesicles: wild-type P2 (solid red line), L27D P2 (dashed red line), MBP at a 1:500 ratio (thick black line) and MBP at a 1:1500 ratio (thin black line). (d) Vesicle-aggregation assay of wild-type (open symbols) and L27D (filled symbols) P2.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

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

doi:10.1107/S1399004713027910

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