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PDBsum entry 3kaa
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Immune system
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PDB id
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3kaa
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Contents |
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* Residue conservation analysis
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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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Structure of tim-3 in complex with phosphatidylserine
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Structure:
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Hepatitis a virus cellular receptor 2. Chain: a, b. Fragment: n-terminal cys-rich domain. Synonym: t-cell immunoglobulin and mucin domain-containing protein 3. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Strain: balb/c. Gene: havcr2, hepatitis a virus cellular receptor 2, tim3, timd3. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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3.00Å
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R-factor:
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0.236
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R-free:
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0.245
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Authors:
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A.Ballesteros,C.Santiago,J.M.Casasnovas
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Key ref:
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R.H.DeKruyff
et al.
(2010).
T cell/transmembrane, Ig, and mucin-3 allelic variants differentially recognize phosphatidylserine and mediate phagocytosis of apoptotic cells.
J Immunol,
184,
1918-1930.
PubMed id:
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Date:
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19-Oct-09
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Release date:
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26-Jan-10
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PROCHECK
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Headers
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References
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Q8VIM0
(HAVR2_MOUSE) -
Hepatitis A virus cellular receptor 2 homolog from Mus musculus
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Seq:
Struc:
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281 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 6 residue positions (black
crosses)
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J Immunol
184:1918-1930
(2010)
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PubMed id:
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T cell/transmembrane, Ig, and mucin-3 allelic variants differentially recognize phosphatidylserine and mediate phagocytosis of apoptotic cells.
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R.H.DeKruyff,
X.Bu,
A.Ballesteros,
C.Santiago,
Y.L.Chim,
H.H.Lee,
P.Karisola,
M.Pichavant,
G.G.Kaplan,
D.T.Umetsu,
G.J.Freeman,
J.M.Casasnovas.
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ABSTRACT
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T cell/transmembrane, Ig, and mucin (TIM) proteins, identified using a congenic
mouse model of asthma, critically regulate innate and adaptive immunity. TIM-1
and TIM-4 are receptors for phosphatidylserine (PtdSer), exposed on the surfaces
of apoptotic cells. Herein, we show with structural and biological studies that
TIM-3 is also a receptor for PtdSer that binds in a pocket on the N-terminal IgV
domain in coordination with a calcium ion. The TIM-3/PtdSer structure is similar
to that of TIM-4/PtdSer, reflecting a conserved PtdSer binding mode by TIM
family members. Fibroblastic cells expressing mouse or human TIM-3 bound and
phagocytosed apoptotic cells, with the BALB/c allelic variant of mouse TIM-3
showing a higher capacity than the congenic C.D2 Es-Hba-allelic variant. These
functional differences were due to structural differences in the BC loop of the
IgV domain of the TIM-3 polymorphic variants. In contrast to fibroblastic cells,
T or B cells expressing TIM-3 formed conjugates with but failed to engulf
apoptotic cells. Together these findings indicate that TIM-3-expressing cells
can respond to apoptotic cells, but the consequence of TIM-3 engagement of
PtdSer depends on the polymorphic variants of and type of cell expressing TIM-3.
These findings establish a new paradigm for TIM proteins as PtdSer receptors and
unify the function of the TIM gene family, which has been associated with asthma
and autoimmunity and shown to modulate peripheral tolerance.
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Links
