User:Daniel Seeman/Alpha-1-antitrypsin

spinqualitylabelsall models PDB ID 1atu1ezxwd.pdb Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1atu, resolution 2.70Å ()
Structural annotation: Resources: CATH : 1Atu002, 1Atu001 InterPro : Ipr000215 Pfam : PF00079 SCOP : d1atu__ UniProt : P01009
Functional annotation: Cellular component: extracellular space extracellular region Biological process: acute-phase response Molecular function: protein binding serine-type endopeptidase inhibitor activity endopeptidase inhibitor activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Alpha-1-antitrypsin (or α1-antitrypsin, A1AT) is an inhibitor of Elastase and 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. Shown is a morph, generated by the Yale Morph Server that shows A1AT going from its inactive form, to the conformation in which it is bound to Trypsin (also shown in the same animation).

Role in diseaseRole in disease

Mutations of MET358 to ARG can lead to a change in specificity in the Elastase binding pocket, essentially turning the M358R mutant of A1AT into a Thrombin inhibitor by generating specificity for this new substrate. This drop in Thrombin levels can lead to hemorrhaging.

See AlsoSee Also

• 1atu
• 1ezx