1wfa
From Proteopedia
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{{STRUCTURE_1wfa| PDB=1wfa | SCENE= }} | {{STRUCTURE_1wfa| PDB=1wfa | SCENE= }} | ||
| - | + | ===WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C=== | |
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| - | + | The line below this paragraph, {{ABSTRACT_PUBMED_7760940}}, adds the Publication Abstract to the page | |
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==About this Structure== | ==About this Structure== | ||
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[[Category: Ice binding protein]] | [[Category: Ice binding protein]] | ||
[[Category: Thermal hysteresis protein]] | [[Category: Thermal hysteresis protein]] | ||
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| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:10:27 2008'' | ||
Revision as of 00:10, 28 July 2008
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 Single protein structure of sequence from Pseudopleuronectes americanus. Full crystallographic information is available from OCA.
Reference
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
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