2ach
From Proteopedia
(New page: 200px<br /> <applet load="2ach" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ach, resolution 2.7Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:2ach.gif|left|200px]]<br /> | + | [[Image:2ach.gif|left|200px]]<br /><applet load="2ach" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ach" size=" | + | |
caption="2ach, resolution 2.7Å" /> | caption="2ach, resolution 2.7Å" /> | ||
'''CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS'''<br /> | '''CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of proteolytically modified human alpha | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2ACH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2ACH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ACH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Grosse, D.]] | [[Category: Grosse, D.]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
| - | [[Category: Laurell, C | + | [[Category: Laurell, C B.]] |
[[Category: Lesjak, M.]] | [[Category: Lesjak, M.]] | ||
[[Category: PO4]] | [[Category: PO4]] | ||
[[Category: proteinase inhibitor]] | [[Category: proteinase inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:26:02 2008'' |
Revision as of 14:26, 21 February 2008
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CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Alpha-1-antichymotrypsin deficiency OMIM:[107280], Cerebrovascular disease, occlusive OMIM:[107280]
About this Structure
2ACH is a Single protein structure of sequence from [1] with as ligand. 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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