5JXA

Crystal structure of ligand-free VRC03 antigen-binding fragment.

5JXA の概要

• エントリーDOI: 10.2210/pdb5jxa/pdb
• 分子名称: VRC03 Heavy chain, VRC03 Light chain, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: hiv-1, cd4 binding site, neutralizing, antibody development, immune system
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49259.15

構造登録者

Zhou, T.,Moquin, S.,Joyce, M.G.,Mascola, J.R.,Kwong, P.D. (登録日: 2016-05-12, 公開日: 2016-07-27, 最終更新日: 2024-10-23)

主引用文献

Davenport, T.M.,Gorman, J.,Joyce, M.G.,Zhou, T.,Soto, C.,Guttman, M.,Moquin, S.,Yang, Y.,Zhang, B.,Doria-Rose, N.A.,Hu, S.L.,Mascola, J.R.,Kwong, P.D.,Lee, K.K.
Somatic Hypermutation-Induced Changes in the Structure and Dynamics of HIV-1 Broadly Neutralizing Antibodies.
Structure, 24:1346-1357, 2016

PubMed Abstract: Antibody somatic hypermutation (SHM) and affinity maturation enhance antigen recognition by modifying antibody paratope structure to improve its complementarity with the target epitope. SHM-induced changes in paratope dynamics may also contribute to antibody maturation, but direct evidence of this is limited. Here, we examine two classes of HIV-1 broadly neutralizing antibodies (bNAbs) for SHM-induced changes in structure and dynamics, and delineate the effects of these changes on interactions with the HIV-1 envelope glycoprotein (Env). In combination with new and existing structures of unmutated and affinity matured antibody Fab fragments, we used hydrogen/deuterium exchange with mass spectrometry to directly measure Fab structural dynamics. Changes in antibody structure and dynamics were positioned to improve complementarity with Env, with changes in dynamics primarily observed at the paratope peripheries. We conclude that SHM optimizes paratope complementarity to conserved HIV-1 epitopes and restricts the mobility of paratope-peripheral residues to minimize clashes with variable features on HIV-1 Env.

PubMed: 27477385
DOI: 10.1016/j.str.2016.06.012

実験手法

X-RAY DIFFRACTION (1.6 Å)