1qmo
From Proteopedia
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'''STRUCTURE OF FRIL, A LEGUME LECTIN THAT DELAYS HEMATOPOIETIC PROGENITOR MATURATION''' | '''STRUCTURE OF FRIL, A LEGUME LECTIN THAT DELAYS HEMATOPOIETIC PROGENITOR MATURATION''' | ||
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[[Category: Moore, J G.]] | [[Category: Moore, J G.]] | ||
[[Category: Wyns, L.]] | [[Category: Wyns, L.]] | ||
| - | [[Category: | + | [[Category: Crosslink]] |
| - | [[Category: | + | [[Category: Hematopoietic progenitor]] |
| - | [[Category: | + | [[Category: Lectin]] |
| - | [[Category: | + | [[Category: Sugar complex]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:27:29 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:27, 3 May 2008
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 Page seeded by OCA on Sat May 3 06:27:29 2008
