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Related Concept Videos

Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can exist in...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Structural Protein Function01:56

Structural Protein Function

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Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...

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Related Experiment Video

Updated: Jun 28, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
07:54

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

Published on: September 20, 2012

Structural basis of sequence-specific collagen recognition by SPARC.

Erhard Hohenester1, Takako Sasaki, Camilla Giudici

  • 1Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom. e.hohenester@imperial.ac.uk

Proceedings of the National Academy of Sciences of the United States of America
|November 18, 2008
PubMed
Summary

SPARC protein binds collagen's GVMGFO motif, revealing a specific "Phe pocket" crucial for molecular recognition. This structural insight advances understanding of collagen interactions in biological processes.

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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

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Last Updated: Jun 28, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
07:54

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Published on: September 20, 2012

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis
07:28

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis

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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
07:03

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

Area of Science:

  • Structural biology
  • Biochemistry
  • Extracellular matrix research

Background:

  • Protein interactions with collagen are vital for cell adhesion and signaling.
  • Limited structural data exists for sequence-specific collagen recognition beyond integrin complexes.
  • A conserved GVMGFO motif (O=4-hydroxyproline) in collagen binds multiple proteins, including SPARC, VWF, and DDR2.

Purpose of the Study:

  • To determine the crystal structure of human SPARC bound to a collagen triple-helical peptide containing the GVMGFO motif.
  • To elucidate the molecular mechanism of SPARC-collagen recognition.

Main Methods:

  • X-ray crystallography at 3.2 Å resolution.
  • Co-crystallization of human SPARC with a 33-residue triple-helical collagen peptide.

Main Results:

  • SPARC binds the GVMGFO motifs of collagen, occluding 720 Ų of surface area.
  • Collagen triple helix structure remains canonical upon SPARC binding.
  • SPARC undergoes significant loop remodeling to form a specific 'Phe pocket' accommodating a phenylalanine residue from the collagen chain.

Conclusions:

  • SPARC utilizes a unique 'Phe pocket' for collagen recognition, distinct from other collagen-binding proteins.
  • This binding mechanism is structurally conserved with collagen-binding integrin I-domains.
  • The findings suggest a common structural basis for GVMGFO motif recognition by VWF and DDR2.