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1wfb

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(New page: 200px<br /><applet load="1wfb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wfb, resolution 1.5&Aring;" /> '''WINTER FLOUNDER ANTIF...)
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[[Image:1wfb.jpg|left|200px]]<br /><applet load="1wfb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1wfb, resolution 1.5&Aring;" />
caption="1wfb, resolution 1.5&Aring;" />
'''WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT-180 DEGREES C'''<br />
'''WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT-180 DEGREES C'''<br />
==Overview==
==Overview==
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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.
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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==
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1WFB 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=1WFB OCA].
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1WFB 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=1WFB OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sicheri, F.]]
[[Category: Sicheri, F.]]
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[[Category: Yang, D.S.C.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:22:24 2007''
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''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


1wfb, resolution 1.5Å

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WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT-180 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

1WFB 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

Page seeded by OCA on Thu Feb 21 15:43:39 2008

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