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Related Concept Videos

Protein Organization01:13

Protein Organization

Overview
Antibody Structure01:10

Antibody Structure

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Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...

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Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
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Solution structure of the alpha-subunit of human chorionic gonadotropin.

P J Erbel1, Y Karimi-Nejad, T De Beer

  • 1Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, The Netherlands.

European Journal of Biochemistry
|March 30, 1999
PubMed
Summary
This summary is machine-generated.

The three-dimensional structure of deglycosylated alpha-subunit human chorionic gonadotropin (hCG) reveals increased disorder and flexibility compared to the intact dimer, due to the absence of beta-subunit interactions.

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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

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Area of Science:

  • Structural Biology
  • Biochemistry
  • Hormone Research

Background:

  • Human chorionic gonadotropin (hCG) is a heterodimeric glycoprotein hormone crucial for pregnancy.
  • Understanding the structural dynamics of individual subunits is essential for elucidating hCG function.
  • The alpha-subunit contains a critical cystine knot motif and glycosylation sites influencing stability.

Purpose of the Study:

  • To determine the three-dimensional solution structure of the deglycosylated alpha-subunit of hCG (dg-alpha hCG).
  • To compare the solution structure of free dg-alpha hCG with its crystal structure in the intact dimer.
  • To investigate the impact of beta-subunit absence on the alpha-subunit's conformation and flexibility.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy (2D homonuclear and heteronuclear 1H, 13C) at natural abundance.
  • Distance geometry and simulated annealing protocols using the XPLOR program package.
  • Modeling of the cystine knot motif and protein-carbohydrate interactions using interproton distance restraints and NOEs.

Main Results:

  • The solution structure of dg-alpha hCG is represented by an ensemble of 27 structures, indicating inherent disorder.
  • Compared to the intact dimer's crystal structure, free dg-alpha hCG exhibits increased structural disorder (residues 33-57) and greater flexibility.
  • Distinct backbone conformations near Val76 and Glu77, and altered arrangements of hairpin loops (20-23 and 70-74) were observed in the free subunit.

Conclusions:

  • The absence of beta-subunit interactions significantly increases the structural disorder and flexibility of the alpha-subunit.
  • The beta-N-acetylglucosamine (GlcNAc) residue at Asn78 is tightly associated with the hydrophobic core, shielding it from solvent.
  • These findings highlight the crucial role of subunit interactions in stabilizing the overall hCG structure and function.