1MOY

Streptavidin Mutant with Osteopontin Hexapeptide Insertion Including RGD

1MOY の概要

• エントリーDOI: 10.2210/pdb1moy/pdb
• 関連するPDBエントリー: 1MEP 1MK5 1MM9 1SWE
• 分子名称: Streptavidin, (4R)-2-METHYLPENTANE-2,4-DIOL (3 entities in total)
• 機能のキーワード: tetramer, biotin-binding protein
• 由来する生物種: Streptomyces avidinii
• 細胞内の位置: Secreted: P22629
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13803.01

構造登録者

Le Trong, I.,McDevitt, T.C.,Nelson, K.E.,Stayton, P.S.,Stenkamp, R.E. (登録日: 2002-09-10, 公開日: 2003-05-06, 最終更新日: 2024-02-14)

主引用文献

Le Trong, I.,McDevitt, T.C.,Nelson, K.E.,Stayton, P.S.,Stenkamp, R.E.
Structural characterization and comparison of RGD cell-adhesion recognition sites engineered into streptavidin.
Acta Crystallogr.,Sect.D, 59:828-834, 2003

PubMed Abstract: The RGD (arginine-glycine-aspartic acid) sequence is found in several important extracellular matrix proteins and serves as an adhesion ligand for members of the integrin family of cell-surface receptors. This sequence and flanking residues from fibronectin or osteopontin have been engineered into an accessible surface loop of streptavidin to create two new streptavidin variants (FN-SA or OPN-SA, respectively) that bind cells through the alpha(v)beta(3) and/or alpha(5)beta(1) integrin receptors. Their crystal structures confirm the design and construction of the mutants and provide evidence about the conformational dynamics of the RGD loops. The loops in the isomorphous crystal structures are involved in crystal-packing interactions and this stabilizes their structures. Even so, the loop in OPN-SA is slightly disordered and two of the residues are not seen in difference electron-density maps. Comparison with other experimentally determined structures of RGD loops in cell-adhesion molecules shows that these loops occupy a large subset of conformational space. This is consistent with the view that RGD loops, at least those involved in cell adhesion, sample a number of structures dynamically, a few of which display high affinity for appropriate receptors.

PubMed: 12777798
DOI: 10.1107/S0907444903004153

実験手法

X-RAY DIFFRACTION (1.55 Å)