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- W1973516851 abstract "The crystal structure of proteolytically modified human α1-antichymotrypsin (ACT), a member of the serpin superfamily, has been solved by Paterson search techniques and refined to an R-factor of 18.0% at 2.7 Å resolution with mean deviations from standard bond lengths and angles of 0.013 Å and 3.1 °, respectively. The final model consists of 374 amino acid residues, 126 solvent molecules and five sugar residues. Asn70 could be identified unambiguously as a glycosylation site and Asn104 is probably also glycosylated. The structure of cleaved ACT is compared with cleaved α1-antitrypsin (α1PI) and with plakalbumin, which are prototypical models for cleaved and intact serpins, respectively. Cleaved ACT is very similar to cleaved α1PI: in particular, it has strand s4A, which is liberated by proteolysis, inserted as the middle strand in β-sheet A. ACT and α1PI differ locally only at sites of insertions, except at the segment s3C-turn-s4C, which is displaced by several ångström units. This region of ACT is involved in DNA binding." @default.
- W1973516851 created "2016-06-24" @default.
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- W1973516851 date "1991-04-01" @default.
- W1973516851 modified "2023-09-23" @default.
- W1973516851 title "Crystal structure of cleaved human α1-antichymotrypsin at 2.7 å resolution and its comparison with other serpins" @default.
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- W1973516851 doi "https://doi.org/10.1016/0022-2836(91)90704-a" @default.
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