2poa

From Proteopedia

(Difference between revisions)

Current revision

Schistosoma mansoni Sm14 Fatty Acid-Binding Protein: improvement of protein stability by substitution of the single Cys62 residue

Structural highlights

2poa is a 1 chain structure with sequence from Blood fluke. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. Stability improvement of the fatty acid binding protein Sm14 from S. mansoni by Cys replacement: structural and functional characterization of a vaccine candidate. Biochim Biophys Acta. 2009 Apr;1794(4):655-62. Epub 2008 Dec 25. PMID:19150418 doi:10.1016/j.bbapap.2008.12.010

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2poa"

@@ Line 1: / Line 1: @@
 ==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=''>
+<StructureSection load='2poa' size='340' side='right'caption='[[2poa]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2poa]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2POA FirstGlance]. <br>
+<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2poa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2poa OCA], [http://pdbe.org/2poa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2poa RCSB], [http://www.ebi.ac.uk/pdbsum/2poa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2poa ProSAT]</span></td></tr>
+</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 ==
-[[http://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).
+[[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]]
@@ Line 29: / Line 29: @@
 ==See Also==
-*[[Fatty acid-binding protein|Fatty acid-binding protein]]
+*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 35: @@
 </StructureSection>
 [[Category: Blood fluke]]
+[[Category: Large Structures]]
 [[Category: Ho, P L]]
 [[Category: Oyama, S]]

2poa

From Proteopedia

Current revision

Schistosoma mansoni Sm14 Fatty Acid-Binding Protein: improvement of protein stability by substitution of the single Cys62 residue

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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