2I83

hyaluronan-binding domain of CD44 in its ligand-bound form

2I83 の概要

• エントリーDOI: 10.2210/pdb2i83/pdb
• NMR情報: BMRB: 5903
• 分子名称: CD44 antigen (1 entity in total)
• 機能のキーワード: link module, cell adhesion
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P16070
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17732.69

構造登録者

Takeda, M.,Ogino, S.,Umemoto, R.,Sakakura, M.,Kajiwara, M.,Sugahara, K.N.,Hayasaka, H.,Miyasaka, M.,Terasawa, H.,Shimada, I. (登録日: 2006-09-01, 公開日: 2006-11-21, 最終更新日: 2024-11-20)

主引用文献

Takeda, M.,Ogino, S.,Umemoto, R.,Sakakura, M.,Kajiwara, M.,Sugahara, K.N.,Hayasaka, H.,Miyasaka, M.,Terasawa, H.,Shimada, I.
Ligand-induced Structural Changes of the CD44 Hyaluronan-binding Domain Revealed by NMR
J.Biol.Chem., 281:40089-40095, 2006

PubMed Abstract: CD44, a major cell surface receptor for hyaluronan (HA), contains a functional domain responsible for HA binding at its N terminus (residues 21-178). Accumulating evidence indicates that proteolytic cleavage of CD44 in its extracellular region (residues 21-268) leads to enhanced tumor cell migration and invasion. Hence, understanding the mechanisms underlying the CD44 proteolytic cleavage is important for understanding the mechanism of CD44-mediated tumor progression. Here we present the NMR structure of the HA-binding domain of CD44 in its HA-bound state. The structure is composed of the Link module (residues 32-124) and an extended lobe (residues 21-31 and 125-152). Interestingly, a comparison of its unbound and HA-bound structures revealed that rearrangement of the beta-strands in the extended lobe (residues 143-148) and disorder of the structure in the following C-terminal region (residues 153-169) occurred upon HA binding, which is consistent with the results of trypsin proteolysis studies of the CD44 HA-binding domain. The order-to-disorder transition of the C-terminal region by HA binding may be involved in the CD44-mediated cell migration.

PubMed: 17085435
DOI: 10.1074/jbc.M608425200

実験手法

SOLUTION NMR