Related Experiment Video
Updated: Aug 27, 2025

14:32
Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
Published on: February 27, 2016
8.3K
Bioinformatic analysis of SIRT7 sequence and structure
Francisco Alejandro Lagunas-Rangel1
1Department of Surgical Sciences, Uppsala University, Uppsala, Sweden.
Journal of Biomolecular Structure & Dynamics
|September 23, 2022
Summary
SIRT7, a crucial protein, shows conserved catalytic domains across species, aiding in understanding its function. This research identifies key residues and structural variations, paving the way for new therapeutic molecules for various diseases.
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Sirtuins are vital conserved proteins regulating cellular processes.
- SIRT7, the least studied sirtuin, impacts health and disease, with altered levels in cardiovascular disease, obesity, and cancer.
- Targeting SIRT7 activity offers therapeutic potential for diverse conditions.
Purpose of the Study:
- To analyze the sequence and structure of SIRT7 orthologs across various organisms using bioinformatics.
- To identify conserved regions and key residues within the SIRT7 catalytic domain.
- To construct a phylogenetic tree and predict 3D structures of SIRT7 orthologs.
Main Methods:
- Bioinformatic analysis of SIRT7 ortholog sequences and structures.
- Identification of conserved catalytic domain residues.
- Phylogenetic analysis of SIRT7 across different taxa.
- Prediction of three-dimensional SIRT7 structures.
Main Results:
- The SIRT7 catalytic domain is highly conserved (83.23% identity) with identified key residues (e.g., D118, Y119, R120).
- Phylogenetic analysis revealed distinct clustering of SIRT7 orthologs from mammals, birds, reptiles, amphibians, fish, insects, and arachnids.
- Predicted 3D structures showed a conserved catalytic core with unique N- and C-terminal regions specific to phylogenetic groups.
Conclusions:
- SIRT7 exhibits significant conservation in its catalytic domain, crucial for its function.
- Phylogenetic and structural analyses provide insights into SIRT7 evolution and diversity.
- Findings support the future development of small molecules targeting SIRT7 for human and animal health benefits.
Related Concept Videos
Protein Organization
6.8K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
The primary structure of a protein is its amino acid sequence....
6.8K
Covalently Linked Protein Regulators
6.9K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
6.9K
Cis-regulatory Sequences
3.1K
3.1K
Sanger Sequencing
756.2K
DNA sequencing is a fundamental technique that is routinely used in the biological sciences. This method can be applied to a range of questions at different scales - from the sequencing of a cloned DNA fragment or the study of a mutation in a gene up to whole-genome sequencing. However, despite the widespread use of sequencing today, it was not until 1977 that Fredrick Sanger and his collaborators developed the chain-termination method to decode DNA sequences. It relies on the separation of a...
756.2K
Conserved Binding Sites
4.3K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.3K
Nucleic Acid Structure
6.4K
The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA...
DNA Structure
DNA...
6.4K

