5DZO

Crystal structure of human T-cell immunoglobulin and mucin domain protein 1

5DZO の概要

• エントリーDOI: 10.2210/pdb5dzo/pdb
• 分子名称: Hepatitis A virus cellular receptor 1, NITRATE ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: receptor, ig v domain, immune system
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Membrane ; Single-pass type I membrane protein : Q96D42
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11993.52

構造登録者

Yuan, S.,Rao, Z.,Wang, X. (登録日: 2015-09-25, 公開日: 2015-11-25, 最終更新日: 2024-11-20)

主引用文献

Yuan, S.,Cao, L.,Ling, H.,Dang, M.,Sun, Y.,Zhang, X.,Chen, Y.,Zhang, L.,Su, D.,Wang, X.,Rao, Z.
TIM-1 acts a dual-attachment receptor for Ebolavirus by interacting directly with viral GP and the PS on the viral envelope.
Protein Cell, 6:814-824, 2015

PubMed Abstract: Ebolavirus can cause hemorrhagic fever in humans with a mortality rate of 50%-90%. Currently, no approved vaccines and antiviral therapies are available. Human TIM1 is considered as an attachment factor for EBOV, enhancing viral infection through interaction with PS located on the viral envelope. However, reasons underlying the preferable usage of hTIM-1, but not other PS binding receptors by filovirus, remain unknown. We firstly demonstrated a direct interaction between hTIM-1 and EBOV GP in vitro and determined the crystal structures of the Ig V domains of hTIM-1 and hTIM-4. The binding region in hTIM-1 to EBOV GP was mapped by chimeras and mutation assays, which were designed based on structural analysis. Pseudovirion infection assays performed using hTIM-1 and its homologs as well as point mutants verified the location of the GP binding site and the importance of EBOV GP-hTIM-1 interaction in EBOV cellular entry.

PubMed: 26487564
DOI: 10.1007/s13238-015-0220-y

実験手法

X-RAY DIFFRACTION (1.301 Å)