Structural insights into the binding of the human receptor for advanced glycation end products (RAGE) by S100B, as revealed by an S100B–RAGE-derived peptide complex

Jensen, J.L.; Indurthi, V.S.K.; Neau, D.B.; Vetter, S.W.; Colbert, C.L.

doi:10.1107/S1399004715004216

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 1
The asymmetric unit contents of the S100B–W61 crystal. (a) Two S100B homodimers and one W61 peptide are visible in the asymmetric unit. Monomers of S100B are shown in shades of green, the W61 peptide is shown in violet and Ca²⁺ ions are shown as black spheres. (b) Final refined 2F_o − F_c electron density (blue mesh) contoured at 1σ above the mean of the composite OMIT map shows the W61 peptide on the surface of S100B chain A in the same orientation as in (a).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 71| Part 5| May 2015| Pages 1176-1183

https://doi.org/10.1107/S1399004715004216

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