1wfa
From Proteopedia
(New page: 200px<br /><applet load="1wfa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wfa, resolution 1.7Å" /> '''WINTER FLOUNDER ANTIF...) |
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| - | [[Image:1wfa.jpg|left|200px]]<br /><applet load="1wfa" size=" | + | [[Image:1wfa.jpg|left|200px]]<br /><applet load="1wfa" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wfa, resolution 1.7Å" /> | caption="1wfa, resolution 1.7Å" /> | ||
'''WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C'''<br /> | '''WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Antifreeze proteins provide fish with protection against the freezing | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1WFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudopleuronectes_americanus Pseudopleuronectes americanus] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1WFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudopleuronectes_americanus Pseudopleuronectes americanus] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WFA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sicheri, F.]] | [[Category: Sicheri, F.]] | ||
| - | [[Category: Yang, D | + | [[Category: Yang, D S.C.]] |
[[Category: NH2]] | [[Category: NH2]] | ||
[[Category: ice binding protein]] | [[Category: ice binding protein]] | ||
[[Category: thermal hysteresis protein]] | [[Category: thermal hysteresis protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:43:39 2008'' |
Revision as of 13:43, 21 February 2008
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WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C
Overview
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.
About this Structure
1WFA is a Single protein structure of sequence from Pseudopleuronectes americanus with as ligand. 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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