1x1v
From Proteopedia
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|PDB= 1x1v |SIZE=350|CAPTION= <scene name='initialview01'>1x1v</scene>, resolution 2.45Å | |PDB= 1x1v |SIZE=350|CAPTION= <scene name='initialview01'>1x1v</scene>, resolution 2.45Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x1v OCA], [http://www.ebi.ac.uk/pdbsum/1x1v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1x1v RCSB]</span> | ||
}} | }} | ||
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[[Category: Surolia, A.]] | [[Category: Surolia, A.]] | ||
[[Category: Vijayan, M.]] | [[Category: Vijayan, M.]] | ||
| - | [[Category: HEZ]] | ||
| - | [[Category: MMA]] | ||
| - | [[Category: ZN]] | ||
[[Category: all beta sheet protein]] | [[Category: all beta sheet protein]] | ||
[[Category: beta prism-i fold]] | [[Category: beta prism-i fold]] | ||
[[Category: mannose specific]] | [[Category: mannose specific]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:43:46 2008'' |
Revision as of 21:43, 30 March 2008
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| , resolution 2.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure Of Banana Lectin- Methyl-Alpha-Mannose Complex
Overview
The crystal structure of a complex of methyl-alpha-D-mannoside with banana lectin from Musa paradisiaca reveals two primary binding sites in the lectin, unlike in other lectins with beta-prism I fold which essentially consists of three Greek key motifs. It has been suggested that the fold evolved through successive gene duplication and fusion of an ancestral Greek key motif. In other lectins, all from dicots, the primary binding site exists on one of the three motifs in the three-fold symmetric molecule. Banana is a monocot, and the three motifs have not diverged enough to obliterate sequence similarity among them. Two Greek key motifs in it carry one primary binding site each. A common secondary binding site exists on the third Greek key. Modelling shows that both the primary sites can support 1-2, 1-3, and 1-6 linked mannosides with the second residue interacting in each case primarily with the secondary binding site. Modelling also readily leads to a bound branched mannopentose with the nonreducing ends of the two branches anchored at the two primary binding sites, providing a structural explanation for the lectin's specificity for branched alpha-mannans. A comparison of the dimeric banana lectin with other beta-prism I fold lectins, provides interesting insights into the variability in their quaternary structure.
About this Structure
1X1V is a Single protein structure of sequence from Musa acuminata. Full crystallographic information is available from OCA.
Reference
Unusual sugar specificity of banana lectin from Musa paradisiaca and its probable evolutionary origin. Crystallographic and modelling studies., Singh DD, Saikrishnan K, Kumar P, Surolia A, Sekar K, Vijayan M, Glycobiology. 2005 Oct;15(10):1025-32. Epub 2005 Jun 15. PMID:15958419
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