1wfa

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(New page: 200px<br /><applet load="1wfa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wfa, resolution 1.7&Aring;" /> '''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"
 
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caption="1wfa, resolution 1.7&Aring;" />
 
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'''WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C'''<br />
 
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==Overview==
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==WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C==
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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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<StructureSection load='1wfa' size='340' side='right'caption='[[1wfa]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1wfa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudopleuronectes_americanus Pseudopleuronectes americanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WFA FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wfa OCA], [https://pdbe.org/1wfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wfa RCSB], [https://www.ebi.ac.uk/pdbsum/1wfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wfa ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ANPA_PSEAM ANPA_PSEAM] Antifreeze proteins lower the blood freezing point.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==About this Structure==
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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<ref>PMID:7760940</ref>
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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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7760940 7760940]
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</div>
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[[Category: Pseudopleuronectes americanus]]
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<div class="pdbe-citations 1wfa" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Sicheri, F.]]
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[[Category: Yang, D.S.C.]]
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[[Category: NH2]]
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[[Category: ice binding protein]]
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[[Category: thermal hysteresis protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:22:19 2007''
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==See Also==
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*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pseudopleuronectes americanus]]
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[[Category: Sicheri F]]
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[[Category: Yang DSC]]

Current revision

WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C

PDB ID 1wfa

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