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Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

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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...
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Mutations01:39

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Mutations01:35

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Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
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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.
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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.
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A mutation is a change in the sequence of bases of DNA or RNA in a genome. Some mutations occur during replication of the genome due to errors made by the polymerase enzymes that replicate DNA or RNA. Unlike DNA polymerase, RNA polymerase is prone to errors because it is not capable of “proofreading” its work. Viruses with RNA-based genomes, like HIV, therefore accrue mutations faster than viruses with DNA-based genomes. Because mutation and recombination provide the raw material...
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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MutHTP: mutations in human transmembrane proteins.

A Kulandaisamy1, S Binny Priya1, R Sakthivel1

  • 1Department of Biotechnology, Bhupat and Jyoti Mehta School of BioSciences, Indian Institute of Technology Madras, Chennai, Tamilnadu, India.

Bioinformatics (Oxford, England)
|February 6, 2018
PubMed
Summary
This summary is machine-generated.

A new database, MutHTP, offers comprehensive data on human transmembrane protein mutations, including their structural context and disease association. This resource addresses limitations in existing mutation datasets for researchers studying protein function and disease.

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Area of Science:

  • Biochemistry
  • Genomics
  • Structural Biology

Background:

  • Existing mutation databases lack structural context and clear disease classification for transmembrane proteins.
  • Limitations include data redundancy, ambiguous annotations, and failure to distinguish between soluble and membrane proteins.

Purpose of the Study:

  • To develop a novel database, MutHTP, for comprehensive analysis of human transmembrane protein mutations.
  • To integrate structural environment and topological information with mutation data.

Main Methods:

  • Curated a dataset of 183,395 disease-associated and 17,827 neutral mutations in human transmembrane proteins.
  • Annotated mutation sites with membrane protein topology, structural environment, and functional features.
  • Developed a user-friendly web interface with search, visualization, and download capabilities.

Main Results:

  • MutHTP provides detailed information on a large set of mutations in human transmembrane proteins.
  • The database incorporates structural and topological data, enhancing mutation analysis.
  • Offers comprehensive data access and visualization tools for researchers.

Conclusions:

  • MutHTP serves as a valuable resource for studying the impact of mutations in transmembrane proteins.
  • The database facilitates research into protein function, disease mechanisms, and drug development.
  • Addresses critical gaps in existing mutation data resources.