期刊
PROTEIN SCIENCE
卷 9, 期 8, 页码 1423-1427出版社
WILEY
DOI: 10.1110/ps.9.8.1423
关键词
apoptosis; crmA; crystal structure; cysteine proteinase; inhibition; serpin; viral; X-ray
资金
- NHLBI NIH HHS [HL49234, HL64013] Funding Source: Medline
- NIGMS NIH HHS [GM47522] Funding Source: Medline
CrmA 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 Chat 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 Angstrom 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 beta sheet A, whose sequence and length are unique to crmA.
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