1XGR

Structure for antibody HyHEL-63 Y33I mutant complexed with hen egg lysozyme

1XGR の概要

• エントリーDOI: 10.2210/pdb1xgr/pdb
• 関連するPDBエントリー: 1XGP 1XGQ 1XGT 1XGU
• 分子名称: antibody kappa light chain, antibody kappa heavy chain, Lysozyme C, ... (4 entities in total)
• 機能のキーワード: hyhel-63, 2.1a crystal structure, y33i mutant, immune system
• 由来する生物種: Mus musculus (mouse); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 60494.20

構造登録者

Li, Y.,Huang, Y.,Swaminathan, C.P.,Smith-Gill, S.J.,Mariuzza, R.A. (登録日: 2004-09-17, 公開日: 2005-09-06, 最終更新日: 2024-11-06)

主引用文献

Li, Y.,Huang, Y.,Swaminathan, C.P.,Smith-Gill, S.J.,Mariuzza, R.A.
Magnitude of the hydrophobic effect at central versus peripheral sites in protein-protein interfaces
Structure, 13:297-307, 2005

PubMed Abstract: Hydrophobic interactions are essential for stabilizing protein-protein complexes, whose interfaces generally consist of a central cluster of hot spot residues surrounded by less important peripheral residues. According to the O-ring hypothesis, a condition for high affinity binding is solvent exclusion from interacting residues. This hypothesis predicts that the hydrophobicity at the center is significantly greater than at the periphery, which we estimated at 21 cal mol(-1) A(-2). To measure the hydrophobicity at the center, structures of an antigen-antibody complex where a buried phenylalanine was replaced by smaller hydrophobic residues were determined. By correlating structural changes with binding free energies, we estimate the hydrophobicity at this central site to be 46 cal mol(-1) A(-2), twice that at the periphery. This context dependence of the hydrophobic effect explains the clustering of hot spots at interface centers and has implications for hot spot prediction and the design of small molecule inhibitors.

PubMed: 15698573
DOI: 10.1016/j.str.2004.12.012

実験手法

X-RAY DIFFRACTION (2.1 Å)