5DZO

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

Summary for 5DZO

• Entry DOI: 10.2210/pdb5dzo/pdb
• Descriptor: Hepatitis A virus cellular receptor 1, NITRATE ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: receptor, ig v domain, immune system
• Biological source: Homo sapiens (Human)
• Cellular location: Membrane ; Single-pass type I membrane protein : Q96D42
• Total number of polymer chains: 1
• Total formula weight: 11993.52

Authors

Yuan, S.,Rao, Z.,Wang, X. (deposition date: 2015-09-25, release date: 2015-11-25, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.301 Å)