1dq1

From Proteopedia

(Difference between revisions)

Revision as of 11:33, 3 August 2017

Calcium;Calcium concanavalin A

Structural highlights

1dq1 is a 1 chain structure with sequence from Canavalia ensiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1dq0, 1dq2, 1dq4, 1dq5, 1dq6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CONA_CANBR] Glucose/D-mannose specific lectin. Has anti-inflammatory activity in rats. Induces histamine release in mast cells from hamster and rat. Induces lymphocyte proliferation and IFNG production. Shows toxicity against the aquatic snail B.glabrata at concentrations higher than 20 ug/ml.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

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 reversible binding of manganese and calcium to concanavalin A determines the carbohydrate binding of the lectin by inducing large conformational changes. These changes are governed by the isomerization of a non-proline peptide bond, Ala-207-Asp-208, positioned in a beta-strand in between the calcium binding site S2 and the carbohydrate specificity-determining loop. The replacement of calcium by manganese allowed us to investigate the structures of the carbohydrate binding, locked state and the inactive, unlocked state of concanavalin A, both with and without metal ions bound. Crystals of unlocked metal-free concanavalin A convert to the locked form with the binding of two Mn(2+) ions. Removal of these ions from the crystals traps metal-free concanavalin A in its locked state, a minority species in solution. The ligation of a metal ion in S2 to unlocked concanavalin A causes bending of the beta-strand foregoing the S2 ligand residues Asp-10 and Tyr-12. This bending disrupts conventional beta-sheet hydrogen bonding and forces the Thr-11 side chain against the Ala-207-Asp-208 peptide bond. The steric strain exerted by Thr-11 is presumed to drive the trans-to-cis isomerization. Upon isomerization, Asp-208 flips into its carbohydrate binding position, and the conformation of the carbohydrate specificity determining loop changes dramatically.

The structural features of concanavalin A governing non-proline peptide isomerization.,Bouckaert J, Dewallef Y, Poortmans F, Wyns L, Loris R J Biol Chem. 2000 Jun 30;275(26):19778-87. PMID:10748006^[8]

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

References

↑ Barral-Netto M, Santos SB, Barral A, Moreira LI, Santos CF, Moreira RA, Oliveira JT, Cavada BS. Human lymphocyte stimulation by legume lectins from the Diocleae tribe. Immunol Invest. 1992 Jul;21(4):297-303. PMID:1398779
↑ Gomes JC, Ferreira RR, Cavada BS, Moreira RA, Oliveira JT. Histamine release induced by glucose (mannose)-specific lectins isolated from Brazilian beans. Comparison with concanavalin A. Agents Actions. 1994 May;41(3-4):132-5. PMID:7524287
↑ Ferreira RR, Cavada BS, Moreira RA, Oliveira JT, Gomes JC. Characteristics of the histamine release from hamster cheek pouch mast cells stimulated by lectins from Brazilian beans and concanavalin A. Inflamm Res. 1996 Sep;45(9):442-7. PMID:8891754
↑ Assreuy AM, Shibuya MD, Martins GJ, De Souza ML, Cavada BS, Moreira RA, Oliveira JT, Ribeiro RA, Flores CA. Anti-inflammatory effect of glucose-mannose binding lectins isolated from Brazilian beans. Mediators Inflamm. 1997;6(3):201-10. PMID:18472821 doi:http://dx.doi.org/10.1080/09629359791695
↑ Dam TK, Cavada BS, Grangeiro TB, Santos CF, de Sousa FA, Oscarson S, Brewer CF. Diocleinae lectins are a group of proteins with conserved binding sites for the core trimannoside of asparagine-linked oligosaccharides and differential specificities for complex carbohydrates. J Biol Chem. 1998 May 15;273(20):12082-8. PMID:9575151
↑ Dam TK, Cavada BS, Grangeiro TB, Santos CF, Ceccatto VM, de Sousa FA, Oscarson S, Brewer CF. Thermodynamic binding studies of lectins from the diocleinae subtribe to deoxy analogs of the core trimannoside of asparagine-linked oligosaccharides. J Biol Chem. 2000 May 26;275(21):16119-26. PMID:10747944 doi:http://dx.doi.org/10.1074/jbc.M000670200
↑ dos Santos AF, Cavada BS, da Rocha BA, do Nascimento KS, Sant'Ana AE. Toxicity of some glucose/mannose-binding lectins to Biomphalaria glabrata and Artemia salina. Bioresour Technol. 2010 Jan;101(2):794-8. doi: 10.1016/j.biortech.2009.07.062., Epub 2009 Sep 17. PMID:19765980 doi:http://dx.doi.org/10.1016/j.biortech.2009.07.062
↑ Bouckaert J, Dewallef Y, Poortmans F, Wyns L, Loris R. The structural features of concanavalin A governing non-proline peptide isomerization. J Biol Chem. 2000 Jun 30;275(26):19778-87. PMID:10748006 doi:http://dx.doi.org/10.1074/jbc.M001251200

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/1dq1"

@@ Line 1: / Line 1: @@
 ==Calcium;Calcium concanavalin A==
 <StructureSection load='1dq1' size='340' side='right' caption='[[1dq1]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dq0|1dq0]], [[1dq2|1dq2]], [[1dq4|1dq4]], [[1dq5|1dq5]], [[1dq6|1dq6]]</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=1dq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dq1 OCA], [http://pdbe.org/1dq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dq1 RCSB], [http://www.ebi.ac.uk/pdbsum/1dq1 PDBsum]</span></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=1dq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dq1 OCA], [http://pdbe.org/1dq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dq1 RCSB], [http://www.ebi.ac.uk/pdbsum/1dq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dq1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN]] D-mannose specific lectin.
+[[http://www.uniprot.org/uniprot/CONA_CANBR CONA_CANBR]] Glucose/D-mannose specific lectin. Has anti-inflammatory activity in rats. Induces histamine release in mast cells from hamster and rat. Induces lymphocyte proliferation and IFNG production. Shows toxicity against the aquatic snail B.glabrata at concentrations higher than 20 ug/ml.<ref>PMID:1398779</ref> <ref>PMID:7524287</ref> <ref>PMID:8891754</ref> <ref>PMID:18472821</ref> <ref>PMID:9575151</ref> <ref>PMID:10747944</ref> <ref>PMID:19765980</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 42: / Line 43: @@
 [[Category: Wyns, L]]
 [[Category: Beta-sheet]]
+[[Category: Calcium]]
 [[Category: Calcium binding site]]
 [[Category: Ion binding site]]

1dq1

From Proteopedia

Revision as of 11:33, 3 August 2017

Calcium;Calcium concanavalin A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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