1wfb
From Proteopedia
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| - | [[ | + | ==WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT-180 DEGREES C== |
| + | <StructureSection load='1wfb' size='340' side='right' caption='[[1wfb]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1wfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudopleuronectes_americanus Pseudopleuronectes americanus]. The December 2009 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Antifreeze Proteins'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2009_12 10.2210/rcsb_pdb/mom_2009_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WFB FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wfa|1wfa]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wfb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wfb RCSB], [http://www.ebi.ac.uk/pdbsum/1wfb PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <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> | |
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==See Also== | ==See Also== | ||
*[[Antifreeze protein|Antifreeze protein]] | *[[Antifreeze protein|Antifreeze protein]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Antifreeze Proteins]] | [[Category: Antifreeze Proteins]] | ||
[[Category: Pseudopleuronectes americanus]] | [[Category: Pseudopleuronectes americanus]] | ||
Revision as of 20:10, 28 September 2014
WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT-180 DEGREES C
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