User:Daniel Seeman/Alpha-1-antitrypsin: Difference between revisions

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more serpin info
remove redundant "in the case"
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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}}
'''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.
'''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.  With 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 02:51, 26 November 2008

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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. With A1AT, as with most members of the Serpin family, the transition from inactive precursor protein to active complex comes after a cleavage event.

ScenesScenes

See AlsoSee Also