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Related Concept Videos

Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

Overview
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
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Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
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Conserved Binding Sites

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 analyses the...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:

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Related Experiment Video

Updated: May 25, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

TM hidden treasure: lectin-like domain.

Kenneth K Wu1

  • 1National Health Research Institutes.

Blood
|February 7, 2012
PubMed
Summary
This summary is machine-generated.

Researchers used recombinant thrombomodulin domain 1 (TMD1) to block Lewis Y antigen (LeY)-mediated angiogenesis. This approach shows promise for controlling tumor growth by targeting specific cancer-related antigens.

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Area of Science:

  • Biochemistry
  • Oncology
  • Immunology

Background:

  • Lewis Y antigen (LeY) is a key carbohydrate antigen implicated in tumor progression and angiogenesis.
  • Thrombomodulin domain 1 (TMD1) is a protein domain with potential anti-angiogenic properties.
  • Targeting LeY-mediated pathways offers a potential strategy for cancer therapy.

Discussion:

  • The study investigates the role of the lectin-like domain of thrombomodulin domain 1 (TMD1) in modulating LeY-mediated biological processes.
  • Recombinant TMD1 was utilized to specifically block the interaction of LeY with its cellular targets.
  • This blockade demonstrated an effect on angiogenesis, a critical process for tumor growth and metastasis.

Key Insights:

  • Recombinant TMD1 effectively inhibits Lewis Y antigen (LeY)-mediated angiogenesis.
  • The lectin-like domain of TMD1 plays a crucial role in this inhibitory action.
  • Targeting LeY-mediated angiogenesis with TMD1 presents a novel therapeutic strategy for cancer treatment.

Outlook:

  • Further research is warranted to explore the therapeutic potential of TMD1 in various cancer types.
  • Investigating the precise molecular mechanisms of TMD1-LeY interaction could lead to drug development.
  • Clinical trials may be considered to evaluate the efficacy and safety of TMD1-based therapies for controlling tumor growth.