期刊
PROTEIN ENGINEERING
卷 16, 期 11, 页码 847-851出版社
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzg102
关键词
aggregation; alpha-crystallin; heat shock protein; molecular chaperone; structure
资金
- NEI NIH HHS [EY 10011] Funding Source: Medline
- NATIONAL EYE INSTITUTE [R01EY010011] Funding Source: NIH RePORTER
The small heat shock protein superfamily, extending over all kingdoms, is characterized by a common core domain with variable N- and C-terminal extensions. The relatively hydrophobic N-terminus plays a critical role in promoting and controlling high-order aggregation, accounting for the high degree of structural variability within the superfamily. The effects of N-terminal volume on aggregation were studied using chimeric and truncated proteins. Proteins lacking the N-terminal region did not aggregate above the tetramers, whereas larger N-termini resulted in large aggregates, consistent with the N-termini packing inside the aggregates. Variation in an extended internal loop differentiates typical prokaryotic and plant superfamily members from their animal counterparts; this implies different geometry in the dimeric building block of high-order aggregates.
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