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Related Concept Videos

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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Protein and Protein Structure

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.
A protein's shape is critical to its function. For example, an enzyme can...
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...
Protein Organization01:24

Protein Organization

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The primary structure of a protein is its amino acid sequence.
Structure of Cadherins01:25

Structure of Cadherins

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...
Blood Studies for Cardiovascular System II: CRP, Hcy, and Cardiac Natriuretic Peptide Markers01:19

Blood Studies for Cardiovascular System II: CRP, Hcy, and Cardiac Natriuretic Peptide Markers

Cardiac biomarkers are critical in diagnosing, prognosing, and managing cardiovascular diseases. Routine measurement of specific biomarkers such as B-type natriuretic peptide (BNP), C-reactive protein (CRP), and homocysteine (Hcy) is common practice in clinical settings to evaluate heart function and predict cardiovascular events.
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High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE
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Three dimensional structure of human C-reactive protein

A K Shrive1, G M Cheetham, D Holden

  • 1Department of Physics, Keele University, Keele, UK.

Nature Structural Biology
|April 1, 1996
PubMed
Summary

The structure of human C-reactive protein reveals how it binds phosphocholine via calcium and a hydrophobic pocket. This understanding offers insights into the protein's biological functions.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Immunology

Background:

  • Human C-reactive protein (CRP) is a classical acute phase reactant.
  • CRP plays a crucial role in the innate immune system.
  • The precise molecular mechanisms of CRP's biological functions are not fully understood.

Purpose of the Study:

  • To elucidate the structural basis of phosphocholine binding by human C-reactive protein.
  • To gain insights into the molecular mechanisms underlying CRP's biological role.

Main Methods:

  • X-ray crystallography was used to determine the structure of human C-reactive protein.
  • Structural analysis focused on identifying key residues and interactions involved in ligand binding.

Main Results:

  • The structure reveals that phosphocholine binding is mediated by calcium ions and a hydrophobic pocket involving Phe 66.
  • The residue Glu 81 is positioned to interact with the choline group.
  • A cleft on the pentameric face, opposite the calcium site, may have a significant functional role.

Conclusions:

  • The determined structure provides a molecular explanation for phosphocholine binding by CRP.
  • These findings offer valuable insights into the biological functions of this conserved plasma protein.