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. 2022 Oct 26;298(12):102645. doi: 10.1016/j.jbc.2022.102645

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© 2022 The Authors

This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

Low-affinity binding to DPP9 is independent of autoproteolysis.A and B, single-cycle kinetic SPR measurements of binding of the monomeric and oligomeric forms of NLRP1-FIIND (wt) protein to immobilized biotin-DPP9. C, SPR analysis of autoproteolysis-deficient NLRP1-FIIND (S1213A) binding to DPP9. D and E, single-cycle kinetic SPR measurement of binding of NLRP1-FIIND (M1184V or M1184V S1213A) to immobilized biotin-DPP9. F, the measurement in D was repeated with 100 μM Val-boroPro (VbP) present in all dilutions of the FIIND domain. DPP9, dipeptidyl peptidase 9; FIIND, function-to-find domain; N/A, not applicable; NLRP1, nucleotide-binding oligomerization domain–like receptor containing a pyrin domain 1; SPR, surface plasmon resonance.