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Related Concept Videos

Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
Tail-anchoring of Proteins in the ER Membrane01:45

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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...
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Aromatic Hydrocarbon Cations: Structural Overview01:18

Aromatic Hydrocarbon Cations: Structural Overview

Cycloheptatriene is a neutral monocyclic unsaturated hydrocarbon that consists of an odd number of carbon atoms and an intervening sp3 carbon in the ring. The three double bonds in the ring correspond to 6 π electrons, which is a Huckel number, and therefore satisfies the criteria of 4n + 2 π electrons. However, the intervening sp3 carbon disrupts the continuous overlap of p orbitals. As a result, cycloheptatriene is not aromatic.
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Termination of Translation01:44

Termination of Translation

The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
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Predicting Molecular Geometry

VSEPR Theory for Determination of Electron Pair Geometries

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Updated: Jun 15, 2026

Folding and Characterization of a Bio-responsive Robot from DNA Origami
07:59

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Published on: December 3, 2015

CTCF terminal segments are unstructured.

Selena R Martinez1, Jj L Miranda

  • 1Department of Cellular and Molecular Pharmacology, University of California, San Francisco, USA.

Protein Science : a Publication of the Protein Society
|March 3, 2010
PubMed
Summary
This summary is machine-generated.

The CCCTC-binding factor (CTCF) protein organizes genome transcription. Its terminal extensions are unstructured and may act as a scaffold for protein assembly at DNA binding sites.

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Area of Science:

  • Genomics
  • Molecular Biology
  • Protein Structure

Background:

  • The CCCTC-binding factor (CTCF) is crucial for genome organization and transcriptional regulation.
  • CTCF mediates interactions between distant DNA elements within and across chromosomes.
  • The protein's structure includes 11 zinc fingers and flanking polypeptide segments with poorly understood functions.

Purpose of the Study:

  • To investigate the structure and potential function of CTCF's terminal polypeptide segments.
  • To explore the role of these extensions in CTCF's scaffolding capabilities.

Main Methods:

  • Purification of recombinant terminal fragments of the CTCF protein.
  • Characterization of the purified fragments' structural properties (e.g., extension, monomeric state, secondary structure content).

Main Results:

  • The purified terminal fragments of CTCF were found to be extended, monomeric, and largely unstructured.
  • These findings suggest a flexible, rather than rigid, conformation for these regions.

Conclusions:

  • The unstructured nature of CTCF's terminal extensions suggests they may serve as flexible scaffolds.
  • These regions, and potentially the entire CTCF protein, could facilitate the assembly of other proteins at specific DNA binding sites, aiding in transcriptional regulation.