1wfa: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1wfa.jpg|left|200px]]<br /><applet load="1wfa" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1wfa, resolution 1.7&Aring;" />
caption="1wfa, resolution 1.7&Aring;" />
'''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, 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 &lt;0112&gt; axes of the (2021) ice planes.
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 &lt;0112&gt; 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WFA OCA].  
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.S.C.]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:22:19 2007''
''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

File:1wfa.jpg


1wfa, resolution 1.7Å

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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 NH2 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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