4NKD

Crystal structure of engineered anti-EE scFv antibody fragment

4NKD の概要

• エントリーDOI: 10.2210/pdb4nkd/pdb
• 関連するPDBエントリー: 1KTR 3NN8 4NKM 4NKO
• 分子名称: Engineered scFv (1 entity in total)
• 機能のキーワード: antibody fragment, eympme binding, immune system, immune system-chaperone complex, immune system/chaperone
• 由来する生物種: Mus musculus (mouse)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 115455.60

構造登録者

Kalyoncu, S.,Hyun, J.,Pai, J.C.,Johnson, J.L.,Etzminger, K.,Jain, A.,Heaner Jr., D.,Molares, I.A.,Truskett, T.M.,Maynard, J.A.,Lieberman, R.L. (登録日: 2013-11-12, 公開日: 2014-03-12, 最終更新日: 2024-11-20)

主引用文献

Kalyoncu, S.,Hyun, J.,Pai, J.C.,Johnson, J.L.,Entzminger, K.,Jain, A.,Heaner, D.P.,Morales, I.A.,Truskett, T.M.,Maynard, J.A.,Lieberman, R.L.
Effects of protein engineering and rational mutagenesis on crystal lattice of single chain antibody fragments.
Proteins, 82:1884-1895, 2014

PubMed Abstract: Protein crystallization is dependent upon, and sensitive to, the intermolecular contacts that assist in ordering proteins into a three-dimensional lattice. Here we used protein engineering and mutagenesis to affect the crystallization of single chain antibody fragments (scFvs) that recognize the EE epitope (EYMPME) with high affinity. These hypercrystallizable scFvs are under development to assist difficult proteins, such as membrane proteins, in forming crystals, by acting as crystallization chaperones. Guided by analyses of intermolecular crystal lattice contacts, two second-generation anti-EE scFvs were produced, which bind to proteins with installed EE tags. Surprisingly, although noncomplementarity determining region (CDR) lattice residues from the parent scFv framework remained unchanged through the processes of protein engineering and rational design, crystal lattices of the derivative scFvs differ. Comparison of energy calculations and the experimentally-determined lattice interactions for this basis set provides insight into the complexity of the forces driving crystal lattice choice and demonstrates the availability of multiple well-ordered surface features in our scFvs capable of forming versatile crystal contacts.

PubMed: 24615866
DOI: 10.1002/prot.24542

実験手法

X-RAY DIFFRACTION (3.303 Å)