5dzo
Crystal structure of human T-cell immunoglobulin and mucin domain protein 1
Structural highlights
FunctionHAVR1_HUMAN May play a role in T-helper cell development and the regulation of asthma and allergic diseases. Receptor for TIMD4 (By similarity). May play a role in kidney injury and repair.[1] (Microbial infection) Acts as a receptor for hepatitis A virus (PubMed:9658108). Acts as a receptor for ebolavirus and marburg virus by binding exposed phosphatidyl-serine at the surface of virion membrane (PubMed:21536871). Acts as a receptor for Dengue virus by binding exposed phosphatidyl-serine at the surface of virion membrane (PubMed:23084921).[2] [3] [4] Publication Abstract from PubMedEbolavirus 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. TIM-1 acts a dual-attachment receptor for Ebolavirus by interacting directly with viral GP and the PS on the viral envelope.,Yuan S, Cao L, Ling H, Dang M, Sun Y, Zhang X, Chen Y, Zhang L, Su D, Wang X, Rao Z Protein Cell. 2015 Oct 20. PMID:26487564[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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