1Q38

Anastellin

1Q38 の概要

• エントリーDOI: 10.2210/pdb1q38/pdb
• 関連するPDBエントリー: 1FNA 1FNF 1FNH 1J8K 2FNB
• 分子名称: Fibronectin (1 entity in total)
• 機能のキーワード: amyloid fibril, anastellin, extracellular matrix, fibronectin type 3 (fn3) domain, dynamic fluctuations, conformational exchange, chaps, cell adhesion
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix: P02751
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10175.41

構造登録者

Briknarova, K.,Akerman, M.E.,Hoyt, D.W.,Ruoslahti, E.,Ely, K.R. (登録日: 2003-07-28, 公開日: 2003-11-04, 最終更新日: 2024-05-22)

主引用文献

Briknarova, K.,Akerman, M.E.,Hoyt, D.W.,Ruoslahti, E.,Ely, K.R.
Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors
J.Mol.Biol., 332:205-215, 2003

PubMed Abstract: Anastellin is a carboxy-terminal fragment of the first FN3 domain from human fibronectin. It is capable of polymerizing fibronectin in vitro, and it displays anti-tumor, anti-metastatic and anti-angiogenic properties in vivo. We have determined the structure of anastellin using nuclear magnetic resonance spectroscopy and identified residues critical for its activity. Anastellin exhibits dynamic fluctuations and conformational exchange in solution. Its overall topology is very similar to the corresponding region of full-length FN3 domains. However, its hydrophobic core becomes solvent-accessible and some of its beta-strands lose their protection against hydrogen bonding to beta-strands from other molecules. These features seem to be relevant for the fibronectin polymerization activity of anastellin and resemble the characteristics of amyloid fibril precursors. We suggest that this analogy is not random and may reflect similarities between fibronectin and amyloid fibril formation.

PubMed: 12946358
DOI: 10.1016/S0022-2836(03)00890-8

実験手法

SOLUTION NMR