Abstract:
: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 A resolution of a lone alpha-helical antifreeze protein from winter flounder, which provides a detailed look at its ice-binding 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 alpha-helical content in solution. We propose an ice-binding model that accounts for the binding specificity of the antifreeze protein along the <0112> axes of the (2021) ice planes.
journal_name
Naturejournal_title
Natureauthors
Sicheri F,Yang DSdoi
10.1038/375427a0subject
Has Abstractpub_date
1995-06-01 00:00:00pages
427-31issue
6530eissn
0028-0836issn
1476-4687journal_volume
375pub_type
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