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PDBsum entry 5dzo
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Immune system
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PDB id
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5dzo
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PDB id:
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| Name: |
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Immune system
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Title:
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Crystal structure of human t-cell immunoglobulin and mucin domain protein 1
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Structure:
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Hepatitis a virus cellular receptor 1. Chain: a. Fragment: unp residues 22-127. Synonym: havcr-1,kidney injury molecule 1,kim-1,t-cell immunoglobulin and mucin domain-containing protein 1,timd-1,t-cell immunoglobulin mucin receptor 1,tim-1,t-cell membrane protein 1. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: havcr1, kim1, tim1, timd1. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.30Å
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R-factor:
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0.157
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R-free:
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0.176
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Authors:
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S.Yuan,Z.Rao,X.Wang
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Key ref:
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S.Yuan
et al.
(2015).
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.
PubMed id:
DOI:
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Date:
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25-Sep-15
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Release date:
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25-Nov-15
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PROCHECK
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Headers
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References
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Q96D42
(HAVR1_HUMAN) -
Hepatitis A virus cellular receptor 1 from Homo sapiens
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Seq:
Struc:
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364 a.a.
107 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Protein Cell
6:814-824
(2015)
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PubMed id:
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TIM-1 acts a dual-attachment receptor for Ebolavirus by interacting directly with viral GP and the PS on the viral envelope.
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S.Yuan,
L.Cao,
H.Ling,
M.Dang,
Y.Sun,
X.Zhang,
Y.Chen,
L.Zhang,
D.Su,
X.Wang,
Z.Rao.
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ABSTRACT
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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.
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Links
