Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
Serpins utilize conformational change to inhibit target proteinases; the price paid for this conformational flexibility is that many undergo temperature-induced polymerization. Despite this thermolability, serpins are present in the genomes of thermophilic prokaryotes, and here we characterize the first such serpin, thermopin. Thermopin is a proteinase inhibitor and, in comparison with human alpha(1)-antitrypsin, possesses enhanced stability at 60 degrees C. The 1.5 A crystal structure reveals novel structural features in regions implicated in serpin folding and stability. Thermopin possesses a C-terminal "tail" that interacts with the top of the A beta sheet and plays an important role in the folding/unfolding of the molecule. These data provide evidence as to how this unusual serpin has adapted to fold and function in a heated environment.
The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment.,Irving JA, Cabrita LD, Rossjohn J, Pike RN, Bottomley SP, Whisstock JC Structure. 2003 Apr;11(4):387-97. PMID:12679017[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Irving JA, Cabrita LD, Rossjohn J, Pike RN, Bottomley SP, Whisstock JC. The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment. Structure. 2003 Apr;11(4):387-97. PMID:12679017
