Structural highlights
Function
[ILEU_HORSE] Thought to be involved in the control of intracellular protein turnover.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of active-site cleaved equine leucocyte elastase inhibitor, a member of the serpin superfamily, has been solved and refined to a crystallographic R-factor of 17.6% at 1.95 A resolution. Despite being an intracellular inhibitor with rather low sequence homology of 30% to human alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor, the three-dimensional structures are very similar, with deviations only at the sites of insertions and few mobile secondary structure elements. The better resolution in comparison with the structures of other cleaved serpins allows a more precise description of the so-called R-state of the serpins.
Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution.,Baumann U, Bode W, Huber R, Travis J, Potempa J J Mol Biol. 1992 Aug 20;226(4):1207-18. PMID:1518052[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Baumann U, Bode W, Huber R, Travis J, Potempa J. Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution. J Mol Biol. 1992 Aug 20;226(4):1207-18. PMID:1518052
