4B3N

Crystal structure of rhesus TRIM5alpha PRY/SPRY domain

Summary for 4B3N

• Entry DOI: 10.2210/pdb4b3n/pdb
• Related: 1ANF 1DMB 1EZ9 1EZO 1EZP 1FQA 1FQB 1FQC 1FQD 1IUD 1JVX 1JVY 1JW4 1JW5 1LAX 1LLS 1MDP 1MDQ 1MPB 1MPC 1MPD 1N3W 1N3X 1NL5 1NMU 1OMP 1PEB 1R6Z 1SVX 1T0K 1Y4C 1YTV 1ZIU 1ZJL 1ZKB 1ZMG 2D21 2H25 2VGQ 2XZ3 3MBP 4AUF 4AUG 4AUH 4MBP
• Related PRD ID: PRD_900001
• Descriptor: MALTOSE-BINDING PERIPLASMIC PROTEIN, TRIPARTITE MOTIF-CONTAINING PROTEIN 5, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: sugar binding protein-ligase complex, sugar binding protein-ligase chimera, sugar binding protein/ligase
• Biological source: ESCHERICHIA COLI; More
• Total number of polymer chains: 2
• Total formula weight: 135613.61

Authors

Yang, H.,Ji, X.,Zhao, Q.,Xiong, Y. (deposition date: 2012-07-25, release date: 2012-10-24, Last modification date: 2023-12-20)

Primary citation

Yang, H.,Ji, X.,Zhao, G.,Ning, J.,Zhao, Q.,Aiken, C.,Gronenborn, A.M.,Zhang, P.,Xiong, Y.
Structural Insight Into HIV-1 Capsid Recognition by Rhesus Trim5Alpha
Proc.Natl.Acad.Sci.USA, 109:18372-, 2012

PubMed Abstract: Tripartite motif protein isoform 5 alpha (TRIM5α) is a potent antiviral protein that restricts infection by HIV-1 and other retroviruses. TRIM5α recognizes the lattice of the retrovirus capsid through its B30.2 (PRY/SPRY) domain in a species-specific manner. Upon binding, TRIM5α induces premature disassembly of the viral capsid and activates the downstream innate immune response. We have determined the crystal structure of the rhesus TRIM5α PRY/SPRY domain that reveals essential features for capsid binding. Combined cryo-electron microscopy and biochemical data show that the monomeric rhesus TRIM5α PRY/SPRY, but not the human TRIM5α PRY/SPRY, can bind to HIV-1 capsid protein assemblies without causing disruption of the capsid. This suggests that the PRY/SPRY domain alone constitutes an important pattern-sensing component of TRIM5α that is capable of interacting with viral capsids of different curvatures. Our results provide molecular insights into the mechanisms of TRIM5α-mediated retroviral restriction.

PubMed: 23091002
DOI: 10.1073/PNAS.1210903109

Experimental method

X-RAY DIFFRACTION (3.3 Å)