The structure of XIAP BIR2: understanding the selectivity of the BIR domains

Lukacs, C.; Belunis, C.; Crowther, R.; Danho, W.; Gao, L.; Goggin, B.; Janson, C.A.; Li, S.; Remiszewski, S.; Schutt, A.; Thakur, M.K.; Singh, S.K.; Swaminathan, S.; Pandey, R.; Tyagi, R.; Gosu, R.; Kamath, A.V.; Kuglstatter, A.

doi:10.1107/S0907444913016284

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 3
(a) Overlay of ATAA (green), SVPI (orange) and AIAV (blue). A combination of peptide movement and rotation of Gln197 allows the protein to accommodate the differently sized P4 residues. Gln197 was observed in two conformations in the SVPI structure. (b) Overlay of SVPI (orange) and AVPI (red). Instead of Gln197 moving away, the peptide is pushed out. (c) Overlay of SVPI (orange) and AMRV (blue). The arginine causes the backbone to shift enough that the hydrogen bond to the Leu207 backbone is lost.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 69| Part 9| September 2013| Pages 1717-1725

https://doi.org/10.1107/S0907444913016284

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