User:Daniel Seeman/Alpha-1-antitrypsin

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(got the file to load from the scene authoring tools... I didn't originally realize that it would take so long for the file to load so I closed my browser after a few minutes.)
(more serpin info)
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{{STRUCTURE_1atu | PDB=1atu1ezxwd.pdb | SCENE=User:Daniel_Seeman/Alpha-1-antitrypsin/437437437437/1}}
{{STRUCTURE_1atu | PDB=1atu1ezxwd.pdb | SCENE=User:Daniel_Seeman/Alpha-1-antitrypsin/437437437437/1}}
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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.
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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. In the case of A1AT, as with most members of the Serpin family, the transition from inactive precursor protein to active complex comes after a cleavage event.
=== Scenes ===
=== Scenes ===

Revision as of 23:50, 25 November 2008

Drag the structure with the mouse to rotate
1atu, resolution 2.70Å ()
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. In the case of A1AT, as with most members of the Serpin family, the transition from inactive precursor protein to active complex comes after a cleavage event.

Scenes

See Also

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Daniel Seeman

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