1wfa
From Proteopedia
Contents |
WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C
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.
Ice-binding structure and mechanism of an antifreeze protein from winter flounder., Sicheri F, Yang DS, Nature. 1995 Jun 1;375(6530):427-31. PMID:7760940
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1wfa is a 2 chain structure of Antifreeze protein with sequence from Pseudopleuronectes americanus. Full crystallographic information is available from OCA.
See Also
Reference
- Sicheri F, Yang DS. Ice-binding structure and mechanism of an antifreeze protein from winter flounder. Nature. 1995 Jun 1;375(6530):427-31. PMID:7760940 doi:http://dx.doi.org/10.1038/375427a0
- Katti MV, Sami-Subbu R, Ranjekar PK, Gupta VS. Amino acid repeat patterns in protein sequences: their diversity and structural-functional implications. Protein Sci. 2000 Jun;9(6):1203-9. PMID:10892812 doi:10.1110/ps.9.6.1203
