1z2f
From Proteopedia
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| - | [[ | + | ==solution structure of CfAFP-501== |
| + | <StructureSection load='1z2f' size='340' side='right' caption='[[1z2f]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1z2f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Choristoneura_fumiferana Choristoneura fumiferana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z2F FirstGlance]. <br> | ||
| + | </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=1z2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z2f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1z2f RCSB], [http://www.ebi.ac.uk/pdbsum/1z2f PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z2/1z2f_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Antifreeze proteins (AFPs) are widely employed by various organisms as part of their overwintering survival strategy. AFPs have the unique ability to suppress the freezing point of aqueous solution and inhibit ice recrystallization through binding to the ice seed crystals and restricting their growth. The solution structure of CfAFP-501 from spruce budworm has been determined by NMR spectroscopy. Our result demonstrates that CfAFP-501 retains its rigid and highly regular structure in solution. Overall, the solution structure is similar to the crystal structure except the N- and C-terminal regions. NMR spin-relaxation experiments further indicate the overall rigidity of the protein and identify a collection of residues with greater flexibilities. Furthermore, Pro91 shows a cis conformation in solution instead of the trans conformation determined in the crystal structure. | ||
| - | + | Solution structure of an antifreeze protein CfAFP-501 from Choristoneura fumiferana.,Li C, Guo X, Jia Z, Xia B, Jin C J Biomol NMR. 2005 Jul;32(3):251-6. PMID:16132825<ref>PMID:16132825</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: Choristoneura fumiferana]] | [[Category: Choristoneura fumiferana]] | ||
[[Category: Jin, C.]] | [[Category: Jin, C.]] | ||
Revision as of 19:44, 28 September 2014
solution structure of CfAFP-501
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