1qmo
From Proteopedia
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|PDB= 1qmo |SIZE=350|CAPTION= <scene name='initialview01'>1qmo</scene>, resolution 3.5Å | |PDB= 1qmo |SIZE=350|CAPTION= <scene name='initialview01'>1qmo</scene>, resolution 3.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qmo OCA], [http://www.ebi.ac.uk/pdbsum/1qmo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qmo RCSB]</span> | ||
}} | }} | ||
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[[Category: Moore, J G.]] | [[Category: Moore, J G.]] | ||
[[Category: Wyns, L.]] | [[Category: Wyns, L.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MAN]] | ||
| - | [[Category: MN]] | ||
[[Category: crosslink]] | [[Category: crosslink]] | ||
[[Category: hematopoietic progenitor]] | [[Category: hematopoietic progenitor]] | ||
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[[Category: sugar complex]] | [[Category: sugar complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:15:55 2008'' |
Revision as of 20:15, 30 March 2008
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| , resolution 3.5Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF FRIL, A LEGUME LECTIN THAT DELAYS HEMATOPOIETIC PROGENITOR MATURATION
Overview
Binding of multivalent glycoconjugates by lectins often leads to the formation of cross-linked complexes. Type I cross-links, which are one-dimensional, are formed by a divalent lectin and a divalent glycoconjugate. Type II cross-links, which are two or three-dimensional, occur when a lectin or glycoconjugate has a valence greater than two. Type II complexes are a source of additional specificity, since homogeneous type II complexes are formed in the presence of mixtures of lectins and glycoconjugates. This additional specificity is thought to become important when a lectin interacts with clusters of glycoconjugates, e.g. as is present on the cell surface. The cryst1al structure of the Glc/Man binding legume lectin FRIL in complex with a trisaccharide provides a molecular snapshot of how weak protein-protein interactions, which are not observed in solution, can become important when a cross-linked complex is formed. In solution, FRIL is a divalent dimer, but in the crystal FRIL forms a tetramer, which allows for the formation of an intricate type II cross-linked complex with the divalent trisaccharide. The dependence on weak protein-protein interactions can ensure that a specific type II cross-linked complex and its associated specificity can occur only under stringent conditions, which explains why lectins are often found forming higher-order oligomers.
About this Structure
1QMO is a Protein complex structure of sequences from Lablab purpureus. Full crystallographic information is available from OCA.
Reference
The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: crystal structure of cross-linked FRIL., Hamelryck TW, Moore JG, Chrispeels MJ, Loris R, Wyns L, J Mol Biol. 2000 Jun 16;299(4):875-83. PMID:10843844
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