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Related Concept Videos

Glycocalyx and its Functions01:14

Glycocalyx and its Functions

The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
Components of...
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
Protein Families02:47

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key locations, protein...

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Updated: Jun 28, 2026

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
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Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Published on: February 5, 2018

P-glycoprotein structure and evolutionary homologies.

I Bosch1, J M Croop

  • 1Harvard Medical School, The Dana-Faber Cancer Institute, Boston, MA, U.S.A.

Cytotechnology
|November 13, 2008
PubMed
Summary
This summary is machine-generated.

Multidrug resistance in cells is linked to P-glycoprotein, a membrane protein family. Analyzing P-glycoprotein structure and homologs aids understanding of drug resistance evolution.

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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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Last Updated: Jun 28, 2026

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
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Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Published on: February 5, 2018

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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Multidrug resistance (MDR) in cell lines is associated with the P-glycoprotein (P-gp) multigene family.
  • Mammalian P-glycoproteins are integral membrane glycoproteins involved in cellular resistance to diverse cytotoxic agents.
  • P-glycoproteins belong to a large superfamily of ATP-dependent transport proteins.

Purpose of the Study:

  • To analyze the structure and evolutionary origins of the P-glycoprotein family.
  • To compare amino acid sequences and intron/exon boundaries of P-glycoprotein homologs across species.

Main Methods:

  • Identification of P-glycoprotein multigene family from multidrug resistant cell lines.
  • Characterization of P-glycoprotein homologs from various species.
  • Comparative analysis of amino acid sequences and intron/exon boundaries.

Main Results:

  • Two classes of mammalian P-glycoproteins confer resistance to a wide array of cytotoxic agents.
  • P-glycoproteins consist of two similar halves, each with six membrane-spanning domains and a nucleotide-binding fold.
  • P-glycoprotein homologs share structural similarities, suggesting a common evolutionary path.

Conclusions:

  • The P-glycoprotein superfamily, including homologs, utilizes ATP for substrate translocation across membranes.
  • Comparative sequence and structural analysis provides insights into the evolution of P-glycoproteins.
  • Understanding P-glycoprotein structure is crucial for developing strategies against multidrug resistance.