9CJ0

The High-Resolution Structure of a Variable Lymphocyte Receptor from Petromyzon marinus Capable of Binding to the Brain Extracellular Matrix

9CJ0 の概要

• エントリーDOI: 10.2210/pdb9cj0/pdb
• 分子名称: Variable Lymphocyte Receptor, 3-[4-(2-HYDROXYETHYL)PIPERAZIN-1-YL]PROPANE-1-SULFONIC ACID, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: adaptive immune system of jawless vertebrates, alternative antigen receptor, leucine-rich repeat, variable lymphocyte receptor, vlr technologies, immune system
• 由来する生物種: Petromyzon marinus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19192.94

構造登録者

Appelt, E.A.,Thoden, J.B.,Shusta, E.V.,Holden, H.M. (登録日: 2024-07-05, 公開日: 2024-07-31, 最終更新日: 2025-03-19)

主引用文献

Appelt, E.A.,Thoden, J.B.,Gehrke, S.A.,Bachmeier, H.D.,Rayment, I.,Shusta, E.V.,Holden, H.M.
The High-Resolution Structure of a Variable Lymphocyte Receptor From Petromyzon marinus Capable of Binding to the Brain Extracellular Matrix.
Proteins, 93:801-811, 2025

PubMed Abstract: Variable lymphocyte receptors (VLRs) are antigen receptors derived from the adaptive immune system of jawless vertebrates such as lamprey (Petromyzon marinus). First discovered in 2004, VLRs have been the subject of numerous biochemical and structural investigations. Due to their unique antigen binding properties, VLRs have been leveraged as possible drug delivery agents. One such VLR, previously identified and referred to as P1C10, was shown to bind to the brain extracellular matrix. Here, we present the high-resolution X-ray crystal structure of this VLR determined to 1.3 Å resolution. The fold is dominated by a six-stranded mixed β-sheet which provides a concave surface for possible antigen binding. Electron density corresponding to a 4-(2-hydroxyethyl)piperazine-1-propanesulfonic acid buffer molecule (HEPPS) was found in this region. By comparing the P1C10 molecular architecture and its buffer binding residues with those of other VLRs previously reported, it was possible to illustrate how this unique class of proteins can accommodate diverse binding partners. Additionally, we provide an analysis of the experimentally determined structure compared to the models generated by the commonly used AlphaFold and iTASSER structure prediction software packages.

PubMed: 39601379
DOI: 10.1002/prot.26768

実験手法

X-RAY DIFFRACTION (1.3 Å)