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Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
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Published on: September 20, 2012

Type V collagen: heterotypic type I/V collagen interactions in the regulation of fibril assembly.

D E Birk1

  • 1Department of Pathology, Anatomy & Cell Biology, Thomas Jefferson University, 1020 Locust Street, JAH 543, Philadelphia, PA 19107, USA. david.birk@mail.tju.edu

Micron (Oxford, England : 1993)
|September 28, 2000
PubMed
Summary

Type V collagen, a minor fibril-forming protein, regulates collagen fibril assembly. Its NH(2)-terminal domains control fibril initiation and growth, impacting tissue development.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Biomaterials Science

Background:

  • Type V collagen is a minor fibril-forming collagen with diverse tissue distribution.
  • Common isoforms include alpha1(V)2 alpha2(V) in the cornea, but other heterotrimeric and homotrimeric forms exist.
  • The precise functional roles and fibrillar organization of various type V collagen isoforms remain largely unelucidated.

Purpose of the Study:

  • To investigate the functional role and fibrillar organization of type V collagen isoforms.
  • To elucidate the mechanism by which type V collagen regulates fibril assembly, particularly in the cornea.
  • To explore the potential tissue-specific roles of different type V collagen isoforms.

Main Methods:

  • Analysis of collagen fibril structure and assembly in corneal tissues.
  • Molecular modeling of type V collagen NH(2)-terminal domains.
  • Investigation of collagen-collagen interactions during fibrillogenesis.

Main Results:

  • Type V collagen co-assembles with type I collagen into heterotypic fibrils, with type V molecules buried within and type I on the surface.
  • The NH(2)-terminal domains of type V collagen are exposed at the fibril surface, influencing fibril assembly.
  • These domains regulate the accretion of collagen molecules, controlling lateral fibril growth and initiating new fibril formation.

Conclusions:

  • Type V collagen's NH(2)-terminal domains are critical regulators of collagen fibril assembly, influencing fibril diameter and density.
  • Different type V collagen isoforms and their aggregate structures likely mediate tissue-specific matrix organization.
  • Understanding these mechanisms is crucial for comprehending tissue development and potential therapeutic interventions.