2ach

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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'''
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===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.
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(as it appears on PubMed at http://www.pubmed.gov), where 2016749 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2016749}}
==About this Structure==
==About this Structure==
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[[Category: Lesjak, M.]]
[[Category: Lesjak, M.]]
[[Category: Proteinase inhibitor]]
[[Category: Proteinase inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:52:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:05:02 2008''

Revision as of 17:05, 28 July 2008

Image:2ach.png

Template:STRUCTURE 2ach

CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS

Template:ABSTRACT PUBMED 2016749

About this Structure

2ACH is a Single protein structure. Full crystallographic information is available from OCA.

Reference

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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