Evaluation of a crystallographic surrogate for kallikrein 5 in the discovery of novel inhibitors for Netherton syndrome

Thorpe, J.H.; Edgar, E.V.; Smith, K.J.; Lewell, X.Q.; Rella, M.; White, G.V.; Polyakova, O.; Nassau, P.; Walker, A.L.; Holmes, D.S.; Pearce, A.C.; Wang, Y.; Liddle, J.; Hovnanian, A.

doi:10.1107/S2053230X19003169

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
(a) Electrostatic surface of KLK5 (generated by CCP4mg; McNicholas et al., 2011

) with the S1, S2, S3, S4, S1′ and S2′ pockets and the active-site residues labelled. The surface was generated from the leupeptin-bound structure (leupeptin is shown in light blue) with PDB code 2psx following re-refinement to correct the peptide conformation of Tyr41. (b) Chemical diagram of GSK144 (4-{[(4-phenyl-1H-imidazol-2-yl)methyl]amino}-2-(pyridine-3-ylmethoxy)benzimidamide). (c) Biochemical assay measurements for GSK144 binding to each enzyme.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 75| Part 5| May 2019| Pages 385-391

https://doi.org/10.1107/S2053230X19003169

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