User:Daniel Seeman/Alpha-1-antitrypsin: Difference between revisions
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Image:1atu 1ezxwd30.pdb |
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{{STRUCTURE_1atu | PDB=1atu | SCENE= }} | {{STRUCTURE_1atu | PDB=1atu 1ezxwd30.pdb | SCENE= }} | ||
'''Alpha-1-antitrypsin''' (or α1-antitrypsin, A1AT) is an inhibitor of [[Trypsin]]. It is a member of the '''Ser'''ine '''P'''rotease '''I'''nhibitor ([[:Category:Serpin|Serpin]]) family, and as such undergoes a conformational change where a loop region becomes ordered as a Beta Strand. In this case Trypsin is inhibited when a covalent bond is formed to A1AT. | '''Alpha-1-antitrypsin''' (or α1-antitrypsin, A1AT) is an inhibitor of [[Trypsin]]. It is a member of the '''Ser'''ine '''P'''rotease '''I'''nhibitor ([[:Category:Serpin|Serpin]]) family, and as such undergoes a conformational change where a loop region becomes ordered as a Beta Strand. In this case Trypsin is inhibited when a covalent bond is formed to A1AT. | ||
Revision as of 01:54, 26 November 2008
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| 1atu, resolution 2.70Å () | |||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as 1ezxwd30.pdb:pdb pdb, 1ezxwd30.pdb:cif mmCIF, 1ezxwd30.pdb:xml xml | ||||||||
Alpha-1-antitrypsin (or α1-antitrypsin, A1AT) is an inhibitor of Trypsin. It is a member of the Serine Protease Inhibitor (Serpin) family, and as such undergoes a conformational change where a loop region becomes ordered as a Beta Strand. In this case Trypsin is inhibited when a covalent bond is formed to A1AT.