View source for 2afp


==THE SOLUTION STRUCTURE OF TYPE II ANTIFREEZE PROTEIN REVEALS A NEW MEMBER OF THE LECTIN FAMILY==
<StructureSection load='2afp' size='340' side='right'caption='[[2afp]], [[NMR_Ensembles_of_Models | 5 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2afp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hemam Hemam]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AFP FirstGlance]. <br>
</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=2afp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2afp OCA], [https://pdbe.org/2afp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2afp RCSB], [https://www.ebi.ac.uk/pdbsum/2afp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2afp ProSAT]</span></td></tr>
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== Function ==
[[https://www.uniprot.org/uniprot/ISP2_HEMAM ISP2_HEMAM]] Antifreeze proteins lower the blood freezing point. 
== 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/af/2afp_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/main_output.php?pdb_ID=2afp ConSurf].
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== Publication Abstract from PubMed ==
A recombinant form of the sea raven type II antifreeze protein (SRAFP) has been produced using the Pichia pastoris expression system. The antifreeze activity of recombinant SRAFP is indistinguishable from that of the wild-type protein. The global fold of SRAFP has been determined by two-dimensional 1H homonuclear and three-dimensional 1H- inverted question mark15N inverted question mark heteronuclear NMR spectroscopy using 785 NOE distance restraints and 47 angular restraints. The molecule folds into one globular domain that consists of two helices and nine beta-strands in two beta-sheets. The structure confirms the proposed existence of five disulfide bonds. The global fold of SRAFP is homologous to C-type lectins and pancreatic stone proteins, even though the sequence identity is only approximately 20%.

The solution structure of type II antifreeze protein reveals a new member of the lectin family.,Gronwald W, Loewen MC, Lix B, Daugulis AJ, Sonnichsen FD, Davies PL, Sykes BD Biochemistry. 1998 Apr 7;37(14):4712-21. PMID:9537986<ref>PMID:9537986</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2afp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hemam]]
[[Category: Large Structures]]
[[Category: Daugulis, A J]]
[[Category: Davies, P L]]
[[Category: Gronwald, W]]
[[Category: Lix, B]]
[[Category: Loewen, M C]]
[[Category: Sonnichsen, F D]]
[[Category: Sykes, B D]]
[[Category: Antifreeze protein]]
[[Category: C-type lectin]]
[[Category: Recombinant sea raven protein]]
[[Category: Solution backbone fold]]