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From Proteopedia
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== Relevance == | == Relevance == | ||
| + | Collagen is the most abundant protein found in the human body (~30% of the protein content in the human body consists of collagen). As stated in the function of collagen, they are found in fibrous tissues in the body including ligaments, blood vessels, bones, the cornea, and the skin. This protein is important as it provides high tensile strength as it is packed side by side to create collagen fibers allowing it to withstand enormous forces without being broken. By forming these fibers, it allows the connection between muscle and bone in organisms through the form of tendons. Since these collagen fibers can withstand a lot of stress without breaking, there has been more research focusing on creating collagen-like fibers that can withstand higher stresses. | ||
== Structural highlights == | == Structural highlights == | ||
Revision as of 21:15, 21 February 2018
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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Contents |
Function
Disease
Relevance
Collagen is the most abundant protein found in the human body (~30% of the protein content in the human body consists of collagen). As stated in the function of collagen, they are found in fibrous tissues in the body including ligaments, blood vessels, bones, the cornea, and the skin. This protein is important as it provides high tensile strength as it is packed side by side to create collagen fibers allowing it to withstand enormous forces without being broken. By forming these fibers, it allows the connection between muscle and bone in organisms through the form of tendons. Since these collagen fibers can withstand a lot of stress without breaking, there has been more research focusing on creating collagen-like fibers that can withstand higher stresses.
Structural highlights
Collagen’s secondary structure is a trimeric three-stranded helix and its tertiary structure is made of left-handed helix structures. It is composed of three polypeptide α-chains which contain a repeated . G is Glycine, X is mostly proline, and Y is mostly hydroxyproline.
Glycine, located at every third position, is essential to the formation of the structure because of its side chain, which is only one hydrogen atom. This allows it to fit into the crowded three-stranded helix. The side chain of glycine interacts with adjacent strands through hydrogen bonding, which helps hold the chains together. Proline and hydroxyproline allow the polypeptide chain to fold into a helix in such a way that three of these chains can be twisted together into a triple helix.
There are made up of three amino acids again with the G-X-Y sequence: Glycine, Arginine, and Phenylalanine. There are three specific binding sites on collagen strands with these specific amino acids that integrins in the extracellular matrix bind onto and identify. These integrins help facilitate the collagen synthesis of the helical structure as well as the interactions between triple helices to form fibrils.
References
1) Karsdal M. A., Leeming D. J., Henriksen K., Bay-Jensen A. Biochemistry of collagens, laminins and elastin: structure, function and biomarkers. London, United Kingdoms: Elsevier Inc.; 2016.
2) Emsley J, Knight C, Farndale R. W., Barnes M. J., Liddington R.C.. Structural basis of collagen recognition by integrin α2ß1. Cell. 2000;101(1): 47-56.
3) Burgeson R. E., Mayne R. (1987). Structure and Function of Collagen Types. Orlando, Florida: Academic Press Inc.; 1987
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
