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Related Concept Videos

Spongy Bone01:09

Spongy Bone

All bones comprise an outer layer of compact bone, and an interior made up of spongy bone tissue, also called cancellous or trabecular bone. In long bones, spongy bone tissue is mainly found in the interior of the epiphyses (broad ends of the bone).
Spongy bone is more porous, and less dense compared to compact bone. It is composed of concentric lamellae that are arranged irregularly to form the trabecular network. In some bones, the spaces between trabeculae contain red marrow, where...
The Bone Matrix01:18

The Bone Matrix

Bone contains a relatively small number of cells entrenched in a matrix of collagen fibers that provide an adherent surface for inorganic salt crystals. Both components of the matrix, organic and inorganic, contribute to the unusual properties of bone. Without collagen, bones would be brittle and shatter easily. Without mineral crystals, bones would flex and provide little support. This can be observed by an experiment: when the minerals of a bone are dissolved by soaking the bone in acid or...
Bone Structure01:55

Bone Structure

Within the skeletal system, the structure of a bone, or osseous tissue, can be exemplified in a long bone, like the femur, where there are two types of osseous tissue: cortical and cancellous.
Bone Formation by Endochondral Ossification01:24

Bone Formation by Endochondral Ossification

Bone formation, or ossification, begins around the sixth to seventh week of embryonic development. Most bones develop from a cartilaginous template through the process of endochondral ossification. Cartilage formation begins when clusters of mesenchymal cells differentiate into chondrocytes. These chondrocytes proliferate rapidly and secrete an extracellular matrix that becomes encased in a membrane called the perichondrium. The resulting cartilage model provides a template that resembles the...
Bone as Supporting Connective Tissue01:23

Bone as Supporting Connective Tissue

Bone tissue forms the internal skeleton of vertebrate animals, providing structure to the body.
Bone Matrix
Bone, or osseous tissue, is a connective tissue that has a large amount of two different types of matrix material. The organic matrix is similar to the matrix material found in other connective tissues, including some amount of collagen and elastic fibers. This gives strength and flexibility to the tissue. The inorganic matrix consists of mineral salts— mostly calcium salts— that give the...
Protein and Protein Structure02:15

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...

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Updated: May 15, 2026

Three-Dimensional Bone Extracellular Matrix Model for Osteosarcoma
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Three-Dimensional Bone Extracellular Matrix Model for Osteosarcoma

Published on: April 12, 2019

A structural and functional model for human bone sialoprotein.

Kevin Vincent1, Marcus C Durrant

  • 1Department of Chemistry, Durham University, South Road, Durham, United Kingdom.

Journal of Molecular Graphics & Modelling
|December 25, 2012
PubMed
Summary
This summary is machine-generated.

A 3D structural model of bone sialoprotein (BSP) was developed using molecular modeling. This model reveals how BSP

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A Human Bone Marrow 3D Model to Investigate the Dynamics and Interactions Between Resident Cells in Physiological or Tumoral Contexts
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A Human Bone Marrow 3D Model to Investigate the Dynamics and Interactions Between Resident Cells in Physiological or Tumoral Contexts

Published on: December 16, 2022

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Three-Dimensional Bone Extracellular Matrix Model for Osteosarcoma
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A Human Bone Marrow 3D Model to Investigate the Dynamics and Interactions Between Resident Cells in Physiological or Tumoral Contexts
09:07

A Human Bone Marrow 3D Model to Investigate the Dynamics and Interactions Between Resident Cells in Physiological or Tumoral Contexts

Published on: December 16, 2022

Area of Science:

  • Biochemistry
  • Biophysics
  • Materials Science

Background:

  • Bone sialoprotein (BSP) is a key extracellular matrix protein involved in bone mineralization.
  • Mature BSP exhibits extensive post-translational modifications and structural flexibility, hindering experimental characterization.
  • Understanding BSP's structure is crucial for elucidating its role in hydroxyapatite nucleation.

Purpose of the Study:

  • To develop a comprehensive 3D structural model of human bone sialoprotein (BSP).
  • To investigate the molecular mechanisms underlying BSP's role in hydroxyapatite nucleation and binding.
  • To explore the interactions between BSP, calcium ions, and hydroxyapatite.

Main Methods:

  • Development of a 3D structural model for BSP using molecular modeling techniques based on literature data.
  • Application of Density Functional Theory (DFT) quantum calculations to analyze Ca(2+) ion binding.
  • Utilizing molecular dynamics simulations to study hydroxyapatite nucleation and crystal binding.

Main Results:

  • A complete 301-amino acid BSP model was generated, featuring phosphorylated serines, sulfated tyrosines, and glycans.
  • A prominent acidic patch on BSP strongly binds Ca(2+) ions, particularly via phosphorylated serines.
  • Molecular dynamics suggest BSP's flexible cationic loops promote hydroxyapatite nucleation by attracting and assembling ions, rather than acting as a rigid template.

Conclusions:

  • The developed 3D model provides insights into BSP's structure-function relationship in bone mineralization.
  • BSP's acidic patch and flexible loops play critical roles in initiating hydroxyapatite crystal formation.
  • This study enhances understanding of the molecular interactions governing bone extracellular matrix assembly.