User:Daniel Seeman/Alpha-1-antitrypsin
From Proteopedia
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'''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. | ||
| - | <applet load=' | + | <applet load='Final' size='300' frame='true' align='right' caption='Morph of [[1atu]] and [[1ezx]]' /> |
=== See Also === | === See Also === | ||
Revision as of 22:33, 25 November 2008
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| 1atu, resolution 2.70Å () | |||||||||
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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.
