3BIB

Tim-4 in complex with phosphatidylserine

Summary for 3BIB

• Entry DOI: 10.2210/pdb3bib/pdb
• Related: 2or7 2or8 2oyp 3BI9 3BIA
• Descriptor: T-cell immunoglobulin and mucin domain-containing protein 4, SODIUM ION, 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE, ... (4 entities in total)
• Functional Keywords: beta barrel, immunoglobulin fold, igv domain, tim, glycoprotein, immunoglobulin domain, membrane, polymorphism, transmembrane, immune system
• Biological source: Mus musculus (house mouse)
• Cellular location: Membrane; Single-pass type I membrane protein (Potential): Q6U7R4
• Total number of polymer chains: 1
• Total formula weight: 13539.48

Authors

Santiago, C.,Ballesteros, A.,Kaplan, G.G.,Freeman, G.J.,Casasnovas, J.M. (deposition date: 2007-11-30, release date: 2008-01-01, Last modification date: 2024-10-30)

Primary citation

Santiago, C.,Ballesteros, A.,Martinez-Munoz, L.,Mellado, M.,Kaplan, G.G.,Freeman, G.J.,Casasnovas, J.M.
Structures of T Cell Immunoglobulin Mucin Protein 4 Show a Metal-Ion-Dependent Ligand Binding Site where Phosphatidylserine Binds.
Immunity, 27:941-951, 2007

PubMed Abstract: The T cell immunoglobulin and mucin domain (TIM) proteins are important regulators of T cell responses. Crystal structures of the murine TIM-4 identified a metal-ion-dependent ligand binding site (MILIBS) in the immunoglobulin (Ig) domain of the TIM family. The characteristic CC' loop of the TIM domain and the hydrophobic FG loop shaped a narrow cavity where acidic compounds penetrate and coordinate to a metal ion bound to conserved residues in the TIM proteins. The structure of phosphatidylserine bound to the Ig domain showed that the hydrophilic head penetrates into the MILIBS and coordinates with the metal ion, whereas the aromatic residues on the tip of the FG loop interacted with the fatty acid chains and could insert into the lipid bilayer. Our results also revealed an important role of the MILIBS in the trafficking of TIM-1 to the cell surface.

PubMed: 18083575
DOI: 10.1016/j.immuni.2007.11.008

Experimental method

X-RAY DIFFRACTION (2.5 Å)