2ach
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CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS
OverviewOverview
The crystal structure of proteolytically modified human alpha, 1-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 A resolution with mean deviations from standard bond lengths and, angles of 0.013 A and 3.1 degrees, 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 alpha 1-antitrypsin (alpha 1 PI) and with plakalbumin, which, are prototypical models for cleaved and intact serpins, respectively., Cleaved ACT is very similar to cleaved alpha 1 PI; in particular, it has, strand s4A, which is liberated by proteolysis, inserted as the middle, strand in beta-sheet A. ACT and alpha 1 PI differ locally only at sites of, insertions, except at the segment s3C-turn-s4C, which is displaced by, several angstrom units. This region of ACT is involved in DNA binding.
DiseaseDisease
Known diseases associated with this structure: Alpha-1-antichymotrypsin deficiency OMIM:[107280], Cerebrovascular disease, occlusive OMIM:[107280]
About this StructureAbout this Structure
2ACH is a Single protein structure of sequence from [1] with PO4 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7 A resolution and its comparison with other serpins., Baumann U, Huber R, Bode W, Grosse D, Lesjak M, Laurell CB, J Mol Biol. 1991 Apr 5;218(3):595-606. PMID:2016749
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