3ZO0

Mouse IgG2a in complex with mouse TRIM21 PRYSPRY

Replaces:  2VOL

Summary for 3ZO0

• Entry DOI: 10.2210/pdb3zo0/pdb
• Descriptor: IG GAMMA-2A CHAIN C REGION, A ALLELE, E3 UBIQUITIN-PROTEIN LIGASE TRIM21, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: immune system-ligase complex, immune system/ligase
• Biological source: MUS MUSCULUS (HOUSE MOUSE); More
• Cellular location: Cytoplasm: Q62191
• Total number of polymer chains: 2
• Total formula weight: 46095.86

Authors

James, L.C. (deposition date: 2013-02-19, release date: 2013-05-22, Last modification date: 2020-07-29)

Primary citation

Keeble, A.H.,Khan, Z.,Forster, A.,James, L.C.
Trim21 is an Igg Receptor that is Structurally, Thermodynamically, and Kinetically Conserved.
Proc.Natl.Acad.Sci.USA, 105:6045-, 2008

PubMed Abstract: The newly identified tripartite motif (TRIM) family of proteins mediate innate immunity and other critical cellular functions. Here we show that TRIM21, which mediates the autoimmune diseases rheumatoid arthritis, systemic lupus erythematosus, and Sjögren's syndrome, is a previously undescribed IgG receptor with a binding mechanism unlike known mammalian Fcgamma receptors. TRIM21 simultaneously targets conserved hot-spot residues on both Ig domains of the Fc fragment using a PRYSPRY domain with a preformed multisite interface. The binding sites on both TRIM21 and Fc are highly conserved to the extent that the proteins are functionally interchangeable through murine, canine, primate, and human species. Pre-steady-state analysis exposes mechanistic conservation at the level of individual residues, which make the same energetic and kinetic contributions to binding despite varying in sequence. Together, our results reveal that TRIM21 is a previously undescribed type of IgG receptor based on a non-Ig scaffold whose interaction at the fundamental level-structural, thermodynamic, and kinetic-is evolutionarily conserved.

PubMed: 18420815
DOI: 10.1073/PNAS.0800159105

Experimental method

X-RAY DIFFRACTION (1.99 Å)