View source for 1wfa


==WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C==
<StructureSection load='1wfa' size='340' side='right'caption='[[1wfa]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ANPA_PSEAM ANPA_PSEAM] Antifreeze proteins lower the blood freezing point.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1wfa" style="background-color:#fffaf0;"></div>

==See Also==
*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudopleuronectes americanus]]
[[Category: Sicheri F]]
[[Category: Yang DSC]]