1wfa: Difference between revisions
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< | ==WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C== | ||
<StructureSection load='1wfa' size='340' side='right'caption='[[1wfa]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
or the | <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]] 1.7Å</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 <0112> 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®/PubMed®, 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: Pseudopleuronectes americanus]] | ||
[[Category: Sicheri F]] | |||
[[Category: Sicheri | [[Category: Yang DSC]] | ||
[[Category: Yang | |||
Latest revision as of 11:25, 2 August 2023
WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C
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