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- W2084030033 abstract "Kex2 is the yeast prototype of a large family of serine proteases that are highly specific for cleavage of their peptide substrates C-terminal to paired basic sites. This paper reports the 2.2 A resolution crystal structure of ssKex2 in complex with an Ac-Arg-Glu-Lys-Arg peptidyl boronic acid inhibitor (R = 19.7, R(free) = 23.4). By comparison of this structure with the structure of the mammalian homologue furin [Henrich, S., et al. (2003) Nat. Struct. Biol. 10, 520-526], we suggest a structural basis for the differences in substrate recognition at the P(2) and P(4) positions between Kex2 and furin and provide a structural rationale for the lack of P(6) recognition in Kex2. In addition, several monovalent cation binding sites are identified, and a mechanism of activation of Kex2 by potassium ion is proposed." @default.
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- W2084030033 date "2004-02-10" @default.
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- W2084030033 title "Structural Basis for Differences in Substrate Selectivity in Kex2 and Furin Protein Convertases<sup>,</sup>" @default.
- W2084030033 cites W2133498598 @default.
- W2084030033 doi "https://doi.org/10.1021/bi035849h" @default.
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