Alpha-1-antitrypsin: Difference between revisions

'''Alpha-1-antitrypsin''' (also known as α1-antitrypsin or A1AT) is an inhibitor of [[Elastase]] and [[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 the substrate protein associates with a loop region on A1AT causing that loop to become ordered as a Beta Strand<ref name="nature_paper">''Nature'' '''455''', 1189-1190 (30 October 2008)</ref>.  In this case Trypsin (the substrate) is inhibited when a covalent bond is formed to A1AT through the newly formed Beta region<ref name="nature_paper" />.  Once bound covalently to its substrate the stability of the A1AT complex goes up drastically, making it essentially "a molecular mousetrap"<ref name="nature_paper" />.  With A1AT, as with most members of the Serpin family, the transition from inactive precursor protein to active complex comes after a cleavage event<ref name="nature_paper" />.  Shown <scene name='User:Daniel_Seeman/Alpha-1-antitrypsin/437437437437/1'>on the right</scene> is a morph, generated by the <span class="plainlinks">[http://molmovdb.mbb.yale.edu/molmovdb/morph/ Yale Morph Server]</span> that shows A1AT going from its inactive form, to the conformation in which it is bound to Trypsin (also shown in the same animation)<ref>The <span class="plainlinks">[http://molmovdb.mbb.yale.edu/molmovdb/morph/ Yale Morph Server]</span></ref>.