1QMO

Structure of FRIL, a legume lectin that delays hematopoietic progenitor maturation

1QMO の概要

• エントリーDOI: 10.2210/pdb1qmo/pdb
• 分子名称: MANNOSE BINDING LECTIN, FRIL, CALCIUM ION, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: lectin, crosslink, hematopoietic progenitor, sugar complex
• 由来する生物種: DOLICHOS LAB LAB (FIELD BEAN); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 109905.05

構造登録者

Hamelryck, T.W.,Moore, J.G.,Chrispeels, M.,Loris, R.,Wyns, L. (登録日: 1999-10-04, 公開日: 1999-10-10, 最終更新日: 2026-03-04)

主引用文献

Hamelryck, T.W.,Moore, J.G.,Chrispeels, M.J.,Loris, R.,Wyns, L.
The Role of Weak Protein-Protein Interactions in Multivalent Lectin-Carbohydrate Binding: Crystal Structure of Cross-Linked Fril
J.Mol.Biol., 299:875-, 2000

PubMed Abstract: 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.

PubMed: 10843844
DOI: 10.1006/JMBI.2000.3785

実験手法

X-RAY DIFFRACTION (3.5 Å)