2poa
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:2poa.png|left|200px]] | ||
- | + | ==Schistosoma mansoni Sm14 Fatty Acid-Binding Protein: improvement of protein stability by substitution of the single Cys62 residue== | |
- | + | <StructureSection load='2poa' size='340' side='right'caption='[[2poa]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[2poa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2POA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2POA 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=2poa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2poa OCA], [https://pdbe.org/2poa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2poa RCSB], [https://www.ebi.ac.uk/pdbsum/2poa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2poa ProSAT]</span></td></tr> | |
- | -- | + | </table> |
- | + | == Function == | |
+ | [[https://www.uniprot.org/uniprot/FABP_SCHMA FABP_SCHMA]] May play a role in the transport of fatty acids. Binds various fatty acids, such as arachidonic, oleic, palmitic and linolenic acid (in vitro). | ||
+ | == 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/po/2poa_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=2poa ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The Schistosoma mansoni fatty acid binding protein (FABP), Sm14, is a vaccine candidate against, S. mansoni and F. hepatica. Previously, we demonstrated the importance of a correct fold to achieve protection in immunized animals after cercariae challenge [[10]. C.R.R. Ramos, R.C.R. Figueredo, T.A. Pertinhez, M.M. Vilar, A.L.T.O. Nascimento, M. Tendler, I. Raw, A. Spisni, P.L. Ho, Gene structure and M20T polymorphism of the Schistosoma mansoni Sm14 fatty acid-binding protein: structural, functional and immunoprotection analysis. J. Biol. Chem. 278 (2003) 12745-12751.]. Here we show that the reduction of vaccine efficacy over time is due to protein dimerization and subsequent aggregation. We produced the mutants Sm14-M20(C62S) and Sm14-M20(C62V) that, as expected, did not dimerize in SDS-PAGE. Molecular dynamics calculations and unfolding experiments highlighted a higher structural stability of these mutants with respect to the wild-type. In addition, we found that the mutated proteins, after thermal denaturation, refolded to their active native molecular architecture as proved by the recovery of the fatty acid binding ability. Sm14-M20(C62V) turned out to be the more stable form over time, providing the basis to determine the first 3D solution structure of a Sm14 protein in its apo-form. Overall, Sm14-M20(C62V) possesses an improved structural stability over time, an essential feature to preserve its immunization capability and, in experimentally immunized animals, it exhibits a protection effect against S. mansoni cercariae infections comparable to the one obtained with the wild-type protein. These facts indicate this protein as a good lead molecule for large-scale production and for developing an effective Sm14 based anti-helminthes vaccine. | ||
- | + | Stability improvement of the fatty acid binding protein Sm14 from S. mansoni by Cys replacement: structural and functional characterization of a vaccine candidate.,Ramos CR, Spisni A, Oyama S Jr, Sforca ML, Ramos HR, Vilar MM, Alves AC, Figueredo RC, Tendler M, Zanchin NI, Pertinhez TA, Ho PL Biochim Biophys Acta. 2009 Apr;1794(4):655-62. Epub 2008 Dec 25. PMID:19150418<ref>PMID:19150418</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 2poa" style="background-color:#fffaf0;"></div> | ||
- | == | + | ==See Also== |
- | + | *[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] | |
- | [[Category: | + | == References == |
- | [[Category: Ho, P L | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: Pertinhez, T A | + | </StructureSection> |
- | [[Category: Ramos, C R.R | + | [[Category: Blood fluke]] |
- | [[Category: Sforca, M L | + | [[Category: Large Structures]] |
- | [[Category: Spisni, A | + | [[Category: Ho, P L]] |
+ | [[Category: Oyama, S]] | ||
+ | [[Category: Pertinhez, T A]] | ||
+ | [[Category: Ramos, C R.R]] | ||
+ | [[Category: Sforca, M L]] | ||
+ | [[Category: Spisni, A]] | ||
[[Category: Fatty acid binding protein]] | [[Category: Fatty acid binding protein]] | ||
[[Category: Lipid binding protein]] | [[Category: Lipid binding protein]] | ||
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[[Category: Site directed mutagenesis]] | [[Category: Site directed mutagenesis]] | ||
[[Category: Vaccine antigen]] | [[Category: Vaccine antigen]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:25:09 2009'' |
Current revision
Schistosoma mansoni Sm14 Fatty Acid-Binding Protein: improvement of protein stability by substitution of the single Cys62 residue
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