1UUH

Hyaluronan binding domain of human CD44

1UUH の概要

• エントリーDOI: 10.2210/pdb1uuh/pdb
• 分子名称: CD44 ANTIGEN (2 entities in total)
• 機能のキーワード: lectin, hyaluronan, extracellular matrix, receptor, link-domain, c- type lectin, sugar-binding
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35390.55

構造登録者

Teriete, P.,Banerji, S.,Noble, M.,Blundell, C.,Wright, A.,Pickford, A.,Lowe, E.,Mahoney, D.,Tammi, M.,Kahmann, J.,Campbell, I.,Day, A.,Jackson, D. (登録日: 2003-12-19, 公開日: 2004-03-04, 最終更新日: 2024-11-06)

主引用文献

Teriete, P.,Banerji, S.,Noble, M.,Blundell, C.,Wright, A.,Pickford, A.,Lowe, E.,Mahoney, D.,Tammi, M.,Kahmann, J.,Campbell, I.,Day, A.,Jackson, D.
Structure of the Regulatory Hyaluronan-Binding Domain in the Inflammatory Leukocyte Homing Receptor Cd44
Mol.Cell, 13:483-, 2004

PubMed Abstract: Adhesive interactions involving CD44, the cell surface receptor for hyaluronan, underlie fundamental processes such as inflammatory leukocyte homing and tumor metastasis. Regulation of such events is critical and appears to be effected by changes in CD44 N-glycosylation that switch the receptor "on" or "off" under appropriate circumstances. How altered glycosylation influences binding of hyaluronan to the lectin-like Link module in CD44 is unclear, although evidence suggests additional flanking sequences peculiar to CD44 may be involved. Here we show using X-ray crystallography and NMR spectroscopy that these sequences form a lobular extension to the Link module, creating an enlarged HA binding domain and a formerly unidentified protein fold. Moreover, the disposition of key N-glycosylation sites reveals how specific sugar chains could alter both the affinity and avidity of CD44 HA binding. Our results provide the necessary structural framework for understanding the diverse functions of CD44 and developing novel therapeutic strategies.

PubMed: 14992719
DOI: 10.1016/S1097-2765(04)00080-2

実験手法

X-RAY DIFFRACTION (2.2 Å)