3PGF

Crystal structure of maltose bound MBP with a conformationally specific synthetic antigen binder (sAB)

3PGF の概要

• エントリーDOI: 10.2210/pdb3pgf/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose-binding periplasmic protein, SAB Heavy Chain, SAB Light Chain, ... (7 entities in total)
• 機能のキーワード: maltodextrin binding protein, fab, antibody fragment, engineered binding protein, maltodextrin binding protein-de novo protein complex, maltodextrin binding protein/de novo protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Periplasm: P0AEX9; Secreted : P0DOX5
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 92840.60

構造登録者

Kossiakoff, A.A.,Duguid, E.M.,Sandstrom, A. (登録日: 2010-11-01, 公開日: 2011-03-09, 最終更新日: 2024-11-06)

主引用文献

Rizk, S.S.,Paduch, M.,Heithaus, J.H.,Duguid, E.M.,Sandstrom, A.,Kossiakoff, A.A.
Allosteric control of ligand-binding affinity using engineered conformation-specific effector proteins.
Nat.Struct.Mol.Biol., 18:437-442, 2011

PubMed Abstract: We describe a phage display methodology for engineering synthetic antigen binders (sABs) that recognize either the apo or the ligand-bound conformation of maltose-binding protein (MBP). sABs that preferentially recognize the maltose-bound form of MBP act as positive allosteric effectors by substantially increasing the affinity for maltose. A crystal structure of a sAB bound to the closed form of MBP reveals the basis for this allosteric effect. We show that sABs that recognize the bound form of MBP can rescue the function of a binding-deficient mutant by restoring its natural affinity for maltose. Furthermore, the sABs can enhance maltose binding in vivo, as they provide a growth advantage to bacteria under low-maltose conditions. The results demonstrate that structure-specific sABs can be engineered to dynamically control ligand-binding affinities by modulating the transition between different conformations.

PubMed: 21378967
DOI: 10.1038/nsmb.2002

実験手法

X-RAY DIFFRACTION (2.1 Å)