Interaction of the amyloid precursor protein-like protein 1 (APLP1) E2 domain with heparan sulfate involves two distinct binding modes

Dahms, S.O.; Mayer, M.C.; Roeser, D.; Multhaup, G.; Than, M.E.

doi:10.1107/S1399004714027114

Figure 5
Electrostatic interactions of heparin and APLP1 E2. The stereoviews show APLP1 E2 chains a and b in the same orientation. The molecular surface is coloured according to the calculated electrostatic potential, which ranges from red (−10 kT/e⁻) to blue (+10 kT/e⁻). Heparin chains are shown as stick models coloured in a gradient according to the crystallographic B factor, which ranges from green (74 Å²) to red (179 Å²). Red arrowheads mark the reducing ends of heparin. (a) Electrostatic interactions of heparin chain a with APLP1 E2. (b) Electrostatic interactions of heparin chain b with APLP1 E2. (c) Structural stabilization of heparan sulfate by APLP1 E2. The dependence of the increase of the melting temperature of APLP1 E2 on the heparin chain length was measured by thermal denaturation assays (Thermofluor assays). The melting temperatures given correspond to the inflection points of the melting curves of APLP1 E2 without heparin and in the presence of saccharides with defined lengths of two (dp2), four (dp4), eight (dp8), 12 (dp12) and 16 (dp16) sugar rings. dp12, which was used for crystallization, is highlighted as a black bar.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 71| Part 3| February 2015| Pages 494-504

doi:10.1107/S1399004714027114

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