User:Daniel Seeman/Alpha-1-antitrypsin: Difference between revisions
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{{STRUCTURE_1atu | PDB=1atu | SCENE= }} | {{STRUCTURE_1atu | PDB=1atu | SCENE= }} | ||
'''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. | '''Alpha-1-antitrypsin''' (or α1-antitrypsin, A1AT) is an inhibitor of trypsin. It is a member of the Serine Protease Inhibitor ([[: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. | ||
=== See Also === | === See Also === | ||
Revision as of 15:17, 25 November 2008
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| 1atu, resolution 2.70Å (default scene) | |||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, 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.
