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| [[Image:2ach.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2ach| PDB=2ach | SCENE= }} | | {{STRUCTURE_2ach| PDB=2ach | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS'''
| | ===CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_2016749}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 2016749 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_2016749}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Lesjak, M.]] | | [[Category: Lesjak, M.]] |
| [[Category: Proteinase inhibitor]] | | [[Category: Proteinase inhibitor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:52:34 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:05:02 2008'' |
