2IWG

COMPLEX BETWEEN THE PRYSPRY DOMAIN OF TRIM21 AND IGG FC

Summary for 2IWG

• Entry DOI: 10.2210/pdb2iwg/pdb
• Related: 1AJ7 1AQK 1D5B 1D5I 1D6V 1DN2 1E4K 1FC1 1FC2 1FCC 1H3T 1H3U 1H3V 1H3W 1H3Y 1HZH 1I7Z 1IIS 1IIX 1L6X 1N7M 1OQX 1T83 2RCS
• Descriptor: IG GAMMA-1 CHAIN C, 52 KDA RO PROTEIN, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: zinc, rna-binding, zinc-finger, dna-binding, ribonucleoprotein, immunoglobulin domain, immunoglobulin c region, systemic lupus erythematosus, polymorphism, glycoprotein, metal-binding
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 4
• Total formula weight: 91180.22

Authors

James, L.C.,Keeble, A.H.,Rhodes, D.A.,Trowsdale, J. (deposition date: 2006-06-30, release date: 2007-03-27, Last modification date: 2020-07-29)

Primary citation

James, L.C.,Keeble, A.H.,Khan, Z.,Rhodes, D.A.,Trowsdale, J.
Structural Basis for Pryspry-Mediated Tripartite Motif (Trim) Protein Function.
Proc.Natl.Acad.Sci.USA, 104:6200-, 2007

PubMed Abstract: The human tripartite motif (TRIM) family comprises 70 members, including HIV restriction factor TRIM5alpha and disease-associated proteins TRIM20 (pyrin) and TRIM21. TRIM proteins have conserved domain architecture but diverse cellular roles. Here, we describe how the C-terminal PRYSPRY domain mediates diverse TRIM functions. The crystal structure of TRIM21 PRYSPRY in complex with its target IgG Fc reveals a canonical binding interface comprised of two discrete pockets formed by antibody-like variable loops. Alanine scanning of this interface has identified the hot-spot residues that control TRIM21 binding to Fc; the same hot-spots control HIV/murine leukemia virus restriction by TRIM5alpha and mediate severe familial Mediterranean fever in TRIM20/pyrin. Characterization of the IgG binding site for TRIM21 PRYSPRY reveals TRIM21 as a superantigen analogous to bacterial protein A and suggests that an antibody bipolar bridging mechanism may contribute to the pathogenic accumulation of anti-TRIM21 autoantibody immune complex in autoimmune disease.

PubMed: 17400754
DOI: 10.1073/PNAS.0609174104

Experimental method

X-RAY DIFFRACTION (2.35 Å)