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1d5s
From Proteopedia
| 1d5s, resolution 3.00Å () | |||||||||
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| Domains: | alpha-1-antitrypsin_like | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
CRYSTAL STRUCTURE OF CLEAVED ANTITRYPSIN POLYMER
Alpha1-antitrypsin deficiency, which can lead to both emphysema and liver disease, is a result of the accumulation of alpha1-antitrypsin polymers within the hepatocyte. A wealth of biochemical and biophysical data suggests that alpha1-antitrypsin polymers form via insertion of residues from the reactive center loop of one molecule into the beta-sheet of another. However, this long-standing hypothesis has not been confirmed by direct structural evidence. Here, we describe the first crystallographic evidence of a beta-strand linked polymer form of alpha1-antitrypsin: the crystal structure of a cleaved alpha1-antitrypsin polymer.
Cleaved antitrypsin polymers at atomic resolution., Dunstone MA, Dai W, Whisstock JC, Rossjohn J, Pike RN, Feil SC, Le Bonniec BF, Parker MW, Bottomley SP, Protein Sci. 2000 Feb;9(2):417-20. PMID:10716194
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1D5S is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Dunstone MA, Dai W, Whisstock JC, Rossjohn J, Pike RN, Feil SC, Le Bonniec BF, Parker MW, Bottomley SP. Cleaved antitrypsin polymers at atomic resolution. Protein Sci. 2000 Feb;9(2):417-20. PMID:10716194
Page seeded by OCA on Tue Feb 17 15:45:10 2009
