1D4N

HUMAN SERUM TRANSFERRIN

1D4N の概要

• エントリーDOI: 10.2210/pdb1d4n/pdb
• 関連するPDBエントリー: 1A8E 1A8F 1D3K
• 分子名称: TRANSFERRIN, CARBONATE ION, FE (III) ION, ... (4 entities in total)
• 機能のキーワード: iron transport, glycoprotein, transferrin, n-lobe, iron-release, carbonate, metal transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P02787
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36515.23

構造登録者

Yang, H.-W.,MacGillivray, R.T.A.,Chen, J.,Luo, Y.,Wang, Y.,Brayer, G.D.,Mason, A.,Woodworth, R.C.,Murphy, M.E.P. (登録日: 1999-10-04, 公開日: 2000-03-01, 最終更新日: 2024-10-30)

主引用文献

Yang, A.H.,MacGillivray, R.T.,Chen, J.,Luo, Y.,Wang, Y.,Brayer, G.D.,Mason, A.B.,Woodworth, R.C.,Murphy, M.E.
Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron.
Protein Sci., 9:49-52, 2000

PubMed Abstract: The X-ray crystallographic structures of two mutants (K206Q and H207E) of the N-lobe of human transferrin (hTF/2N) have been determined to high resolution (1.8 and 2.0 A, respectively). Both mutant proteins bind iron with greater affinity than native hTF/2N. The structures of the K206Q and H207E mutants show interactions (both H-bonding and electrostatic) that stabilize the interaction of Lys296 in the closed conformation, thereby stabilizing the iron bound forms.

PubMed: 10739246

実験手法

X-RAY DIFFRACTION (2 Å)