Structural highlights
Function[IELA_ASPFU] Elastase inhibitor. Non-competitive inhibitor of A.fumigatus elastase with a Ki of 1.6 nM. Inhibits the fibrinogenase and collagenase activities of A.fumigatus elastase. Inhibitor of A.flavus elastase and human leukocyte elastase, and weakly inhibits porcine pancreatic elastase. Does not inhibit elastase from P.aeruginosa or C.atrox venom. Publication Abstract from PubMedElastase from Aspergillus sp. is an important factor for aspergillosis. AFUEI is an inhibitor of the elastase derived from Aspergillus fumigatus. AFUEI is a member of the I78 inhibitor family, and has a high inhibitory activity against elastases of Aspergillus fumigatus and Aspergillus flavus, human neutrophil elastase and bovine chymotrypsin, but does not inhibit bovine trypsin. Here we report the crystal structure of AFUEI in two crystal forms. AFUEI is a wedge-shaped protein composed of an extended loop and a scaffold protein core. The structure of AFUEI shows remarkable similarity to serine protease inhibitors of the potato inhibitor I family, although they are classified into different inhibitor families. A structural comparison with the potato I family inhibitors suggests that the extended loop of AFUEI corresponds to the binding loop of the potato inhibitor I family and AFUEI inhibits its cognate proteases through the same mechanism as the Potato I family inhibitors. X-ray structure analysis and characterization of AFUEI, an elastase inhibitor from Aspergillus fumigatus.,Sakuma M, Imada K, Okumura Y, Uchiya KI, Yamashita N, Ogawa K, Hijikata A, Shirai T, Homma M, Nikai T J Biol Chem. 2013 May 2. PMID:23640894[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 21:57, 24 December 2014.