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2.9 A STRUCTURE OF CLEAVED VIRAL SERPIN CRMA
Structural highlights
FunctionSPI2_CWPXB Specific and potent inhibitor of the interleukin-1-beta converting enzyme (ICE) thereby suppressing an interleukin-1 beta response to infection. The inhibition of ICE by crmA is an example of a "cross-class" interaction, in which a serpin inhibits a non-serine proteinase. Also inhibits granzyme B.[1] [2] 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 PubMedCrmA is an unusual viral serpin that inhibits both cysteine and serine proteinases involved in the regulation of host inflammatory and apoptosis processes. It differs from other members of the serpin superfamily by having a reactive center loop that is one residue shorter, and by its apparent inability to form SDS-stable covalent complexes with cysteine proteinases. To obtain insight into the inhibitory mechanism of crmA, we determined the crystal structure of reactive center loop-cleaved crmA to 2.9 A resolution. The structure, which is the first of a viral serpin, suggests that crmA can inhibit cysteine proteinases by a mechanism analogous to that used by other serpins against serine proteinases. However, one striking difference from other serpins, which may be significant for in vivo function, is an additional highly charged antiparallel strand for b sheet A, whose sequence and length are unique to crmA. Crystal structure of viral serpin crmA provides insights into its mechanism of cysteine proteinase inhibition.,Simonovic M, Gettins PGW, Volz K Protein Sci. 2000 Aug;9(8):1423-7. PMID:10975564[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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