1qmo: Difference between revisions
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'''STRUCTURE OF FRIL, A LEGUME LECTIN THAT DELAYS HEMATOPOIETIC PROGENITOR MATURATION''' | {{Structure | ||
|PDB= 1qmo |SIZE=350|CAPTION= <scene name='initialview01'>1qmo</scene>, resolution 3.5Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF FRIL, A LEGUME LECTIN THAT DELAYS HEMATOPOIETIC PROGENITOR MATURATION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1QMO is a [ | 1QMO is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Lablab_purpureus Lablab purpureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMO OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10843844 10843844] | ||
[[Category: Lablab purpureus]] | [[Category: Lablab purpureus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: sugar complex]] | [[Category: sugar complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:39:45 2008'' | ||
Revision as of 11:39, 20 March 2008
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| 1qmo, resolution 3.5Å | |||||||||||||
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| Ligands: | MAN, CA and MN | ||||||||||||
| 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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