Ice-binding structure and mechanism of an antifreeze protein from winter flounder.
摘要：
ANTIFREEZE proteins provide fish with protection against the freezing effect of polar environments by binding to ice surfaces and inhibiting growth of ice crystals. We present the X-ray crystal structure at 1.5 resolution of a lone α-helical antifreeze protein from winter flounder, which provides a detailed look at its icebinding features. These consist of four repeated ice-binding motifs, the side chains of which are inherently rigid or restrained by pair-wise side-chain interactions to form a flat binding surface. Elaborate amino- and carboxy-terminal cap structures are also present, which explain the protein's rich α-helical content in solution. We propose an ice-binding model that accounts for the binding specificity of the antifreeze protein along the axes of the {2021} ice planes 1 .
展开
DOI：
10.1038/375427a0
被引量：
年份：
1995
Nature
Springer
Nature
(全网免费下载)
EBSCO
掌桥科研
查看更多
万方医学
Semantic Scholar
dx.doi.org
NCBI
NCBI
Europe PMC
NRC Research Press
JBC
ui.adsabs.harvard.edu
adsabs.harvard.edu
ProQuest
ResearchGate
EBSCO
EBSCO
scripts.iucr.org
plantphysiol.org
hdl.handle.net
rsta.royalsocietypublishing.org
repository.tue.nl
macsphere.mcmaster.ca
(全网免费下载)
cheric.org
elifesciences.org
digitalcommons.mcmaster.ca
readcube.com
jeb.biologists.org
pdb.org
rcsb.org
mendeley.com
onAcademic
narcis.nl
Nature
(全网免费下载)
macsphere.mcmaster.ca
(全网免费下载)
通过文献互助平台发起求助，成功后即可免费获取论文全文。
相似文献
参考文献
引证文献
辅助模式
引用
文献可以批量引用啦~
欢迎点我试用！
