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| | <StructureSection load='3cqo' size='340' side='right'caption='[[3cqo]], [[Resolution|resolution]] 2.32Å' scene=''> | | <StructureSection load='3cqo' size='340' side='right'caption='[[3cqo]], [[Resolution|resolution]] 2.32Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3cqo]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Morone_saxatilis Morone saxatilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CQO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3CQO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3cqo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Morone_saxatilis Morone saxatilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CQO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.32Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k12|1k12]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3cqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cqo OCA], [http://pdbe.org/3cqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cqo RCSB], [http://www.ebi.ac.uk/pdbsum/3cqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cqo ProSAT]</span></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=3cqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cqo OCA], [https://pdbe.org/3cqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cqo RCSB], [https://www.ebi.ac.uk/pdbsum/3cqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cqo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2LK81_MORSA Q2LK81_MORSA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Morone saxatilis]] | | [[Category: Morone saxatilis]] |
| - | [[Category: Amzel, L M]] | + | [[Category: Amzel LM]] |
| - | [[Category: Bianchet, M A]] | + | [[Category: Bianchet MA]] |
| - | [[Category: F-lectin]]
| + | |
| - | [[Category: Fucolectin]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
Q2LK81_MORSA
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 plasma of the striped bass Morone saxatilis contains a fucose-specific lectin (MsaFBP32) that consists of two F-type carbohydrate recognition domains (CRDs) in tandem. The crystal structure of the complex of MsaFBP32 with l-fucose reported here shows a cylindrical 81-A-long and 60-A-wide trimer divided into two globular halves: one containing N-terminal CRDs (N-CRDs) and the other containing C-terminal CRDs (C-CRDs). The resulting binding surfaces at the opposite ends of the cylindrical trimer have the potential to cross-link cell surface or humoral carbohydrate ligands. The N-CRDs and C-CRDs of MsaFBP32 exhibit significant structural differences, suggesting that they recognize different glycans. Analysis of the carbohydrate binding sites provides the structural basis for the observed specificity of MsaFBP32 for simple carbohydrates and suggests that the N-CRD recognizes more complex fucosylated oligosaccharides and with a relatively higher avidity than the C-CRD. Modeling of MsaFBP32 complexed with fucosylated glycans that are widely distributed in prokaryotes and eukaryotes rationalizes the observation that binary tandem CRD F-type lectins function as opsonins by cross-linking "non-self" carbohydrate ligands and "self" carbohydrate ligands, such as sugar structures displayed by microbial pathogens and glycans on the surface of phagocytic cells from the host.
Structure and specificity of a binary tandem domain F-lectin from striped bass (Morone saxatilis).,Bianchet MA, Odom EW, Vasta GR, Amzel LM J Mol Biol. 2010 Aug 13;401(2):239-52. Epub 2010 Jun 16. PMID:20561530[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bianchet MA, Odom EW, Vasta GR, Amzel LM. Structure and specificity of a binary tandem domain F-lectin from striped bass (Morone saxatilis). J Mol Biol. 2010 Aug 13;401(2):239-52. Epub 2010 Jun 16. PMID:20561530 doi:10.1016/j.jmb.2010.06.018
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