Collagen Structure & Function
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==Introduction== | ==Introduction== | ||
- | Collagen is a member of a naturally occurring protein family. It is one of the most plentiful proteins present in mammals and is responsible for performing a variety of biological functions. It often works in conjuction with other important proteins such as keratin and elastin. | + | Collagen is a member of a naturally occurring protein family. It is one of the most plentiful proteins present in [[mammals]] and is responsible for performing a variety of biological functions. It often works in conjuction with other important proteins such as [[keratin]] and [[elastin]]. |
==Molecular Structure== | ==Molecular Structure== |
Revision as of 03:54, 24 March 2010
Contents |
Collagen
Introduction
Collagen is a member of a naturally occurring protein family. It is one of the most plentiful proteins present in mammals and is responsible for performing a variety of biological functions. It often works in conjuction with other important proteins such as keratin and elastin.
Molecular Structure
Collagen takes the form of a triple helix which is stabilized by hydrogen bonding. Each of it's α-helices are enclosed by a hydration cylinder. The molecule itself is approxiametly 1-2nm in diameter and 300nm in length.
Function
There are currently close to 30 different types of collagen that have been identified. The most abundant type of collagen present in the human body is that of Type I with significant amounts of Type II,III and IV also accounted for.
- Type I- found in bones,tendons,organs
- Type II-found mainly in cartilage
- Type III-found mainly in reticular fibres
- Type IV-found in the basement membrane of cell membranes
- Type V-found in hair
Collagen-Related Disorders
There are many types of disorders associated with collagen. These include:
- Elhers-Danlos Syndrome
- Alport Syndrome
- Osteogenesis imperfecta
- Chondrodysplasias
- Atopic Dermatitis
References
Bella J, Eaton M, Brodsky B, Berman HM Crystal and molecular structure of a collagen-like peptide at 1.9A resolution Science v266, p.75-81
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1cag, resolution 1.85Å () | |||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Proteopedia Page Contributors and Editors (what is this?)
Daman K. Kandola, Alexander Berchansky, David Canner, Andrea Gorrell, Luis Netto