6VIT

The Crystal Structure of Apo Domain-Swapped dimer Q108K:T51D:I32C Variant of HCRBPII with an Engineered Disulfide Bond

6VIT の概要

• エントリーDOI: 10.2210/pdb6vit/pdb
• 分子名称: Retinol-binding protein 2 (2 entities in total)
• 機能のキーワード: domain swapped trimer, ilbp, lipid binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31204.95

構造登録者

Ghanbarpour, A.,Geiger, J. (登録日: 2020-01-13, 公開日: 2020-08-19, 最終更新日: 2024-10-16)

主引用文献

Ghanbarpour, A.,Santos, E.M.,Pinger, C.,Assar, Z.,Hossaini Nasr, S.,Vasileiou, C.,Spence, D.,Borhan, B.,Geiger, J.H.
Human Cellular Retinol Binding Protein II Forms a Domain-Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering.
Chembiochem, 21:3192-3196, 2020

PubMed Abstract: Domain-swapping is a mechanism for evolving new protein structure from extant scaffolds, and has been an efficient protein-engineering strategy for tailoring functional diversity. However, domain swapping can only be exploited if it can be controlled, especially in cases where various folds can coexist. Herein, we describe the structure of a domain-swapped trimer of the iLBP family member hCRBPII, and suggest a mechanism for domain-swapped trimerization. It is further shown that domain-swapped trimerization can be favored by strategic installation of a disulfide bond, thus demonstrating a strategy for fold control. We further show the domain-swapped trimer to be a useful protein design template by installing a high-affinity metal binding site through the introduction of a single mutation, taking advantage of its threefold symmetry. Together, these studies show how nature can promote oligomerization, stabilize a specific oligomer, and generate new function with minimal changes to the protein sequence.

PubMed: 32608180
DOI: 10.1002/cbic.202000405

実験手法

X-RAY DIFFRACTION (3.2 Å)