Related Experiment Video

Updated: May 20, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

Structure of the rhesus monkey TRIM5α PRYSPRY domain, the HIV capsid recognition module

Nikolaos Biris1, Yang Yang, Alexander B Taylor

  • 1Department of Biochemistry, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA.

Proceedings of the National Academy of Sciences of the United States of America
|August 1, 2012
PubMed

Insights

The TRIM5α protein restricts HIV by binding to its capsid. Structural analysis reveals how rhesus monkey TRIM5α interacts with the HIV capsid, offering insights into viral restriction mechanisms.

Area of Science:

  • Structural biology
  • Virology
  • Immunology

Background:

  • Tripartite motif protein TRIM5α (TRIM5α) inhibits retroviral replication post-entry.
  • Species-specific activity of TRIM5α is linked to variations in its C-terminal B30.2/PRYSPRY domain.

Purpose of the Study:

  • To determine the high-resolution structure of the rhesus monkey TRIM5α PRYSPRY domain.
  • To identify the structural features mediating TRIM5α interaction with the HIV capsid.

Main Methods:

  • X-ray crystallography to obtain high-resolution structure of the TRIM5α PRYSPRY domain.
  • Structural analysis to map the capsid-binding interface.

Main Results:

  • A high-resolution structure of the rhesus monkey TRIM5α PRYSPRY domain was determined.
  • An extensive capsid-binding interface was identified on a structurally divergent face of the protein, involving hypervariable loop segments.
  • The interaction mechanism resembles IgM antibody antigen recognition, involving flexible loops and multiple epitopes.

Conclusions:

  • TRIM5α evolution is driven by its binding specificity to viral capsids.
  • Structural plasticity and multi-epitope recognition contribute to TRIM5α's broad retroviral restriction and resistance to capsid mutations.

More Related Videos

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods10:40

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

Analysis of Simian Immunodeficiency Virus-specific CD8+ T-cells in Rhesus Macaques by Peptide-MHC-I Tetramer Staining06:25

Analysis of Simian Immunodeficiency Virus-specific CD8+ T-cells in Rhesus Macaques by Peptide-MHC-I Tetramer Staining

Published on: December 23, 2016

Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Viral Structure00:56

Viral Structure

Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
Retroviruses02:33

Retroviruses

Retroviruses and retrotransposons both insert copies of their genetic elements into the genome of the host cell. Thus, the viral genes are passed on when the host genome is replicated or translated. A typical retroviral DNA sequence contains 3-4 genes that encode the different proteins required for its structural assembly and function as a molecular parasite. This DNA is transcribed into a single mRNA, which is very similar in structure to conventional mRNAs, i.e., it is capped at the 5’...
Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.