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From Proteopedia
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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. | 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 binding sites made up of three amino acids: | + | There are <scene name='77/777681/Binding_site/1'>binding sites</scene> 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. |
Revision as of 21:14, 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
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
