THGS: a web-based database of Transmembrane Helices in Genome Sequences
S A Fernando1, P Selvarani, Soma Das
1Bioinformatics Centre, Indian Institute of Science, Bangalore 560 012, India.
Nucleic Acids Research
|December 19, 2003
Summary
The Transmembrane Helices in Genome Sequences (THGS) database identifies transmembrane helices in gene sequences. It allows motif searching across multiple protein and structure databases, aiding in biological research.
Area of Science:
- Bioinformatics
- Structural Biology
- Genomics
Background:
- Transmembrane proteins play crucial roles in cellular functions.
- Identifying transmembrane helices is essential for understanding protein structure and function.
- Existing databases may lack comprehensive tools for searching and visualizing these elements.
Purpose of the Study:
- To develop an interactive web-based database for identifying transmembrane helices in gene sequences.
- To provide tools for searching sequence motifs within transmembrane and globular proteins.
- To enable visualization of 3D protein structures for queried motifs.
Main Methods:
- Development of the Transmembrane Helices in Genome Sequences (THGS) database.
- Integration with Genome Database (GDB), Swiss-Prot, PIR, and Protein Data Bank (PDB).
- Utilization of RASMOL for 3D structure visualization.
Main Results:
- The THGS database enables searching for transmembrane helices in user-specified gene sequences.
- Motif searching is supported across multiple sequence and structural databases.
- Users can visualize 3D structures of identified motifs if available in PDB.
Conclusions:
- THGS offers a valuable, up-to-date resource for researchers studying transmembrane proteins.
- The database facilitates the exploration of sequence motifs and their structural correlates.
- Free web accessibility enhances its utility in bioinformatics and structural biology research.
Related Concept Videos
Globular and Fibrous Proteins
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Single-pass Transmembrane Proteins
Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
Evolutionary Relationships through Genome Comparisons
Genome comparison is one of the excellent ways to interpret the evolutionary relationships between organisms. The basic principle of genome comparison is that if two species share a common feature, it is likely encoded by the DNA sequence conserved between both species. The advent of genome sequencing technologies in the late 20th century enabled scientists to understand the concept of conservation of domains between species and helped them to deduce evolutionary relationships across diverse...
Insertion of Single-pass Transmembrane Proteins in the RER
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Insertion of Multi-pass Transmembrane Proteins in the RER
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Multi-pass Transmembrane Proteins and β-barrels
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...


