Fibrillin
| fibrillin 1 | |
|---|---|
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Crystallographic structure of the cbEGF9-hybrid2-cbEGF10 region of human fibrillin 1.[1]
|
|
| Identifiers | |
| Symbol | FBN1 |
| Alt. symbols | FBN, MFS1, WMS |
| Entrez | 2200 |
| HUGO | 3603 |
| OMIM | 134797 |
| PDB | 2W86 |
| RefSeq | NM_000138 |
| UniProt | P35555 |
| Other data | |
| Locus | Chr. 15 q21.1 |
| fibrillin 2 | |
|---|---|
| Identifiers | |
| Symbol | FBN2 |
| Alt. symbols | CCA |
| Entrez | 2201 |
| HUGO | 3604 |
| OMIM | 121050 |
| RefSeq | NM_001999 |
| UniProt | P35556 |
| Other data | |
| Locus | Chr. 5 q23-q31 |
| fibrillin 3 | |
|---|---|
| Identifiers | |
| Symbol | FBN3 |
| Entrez | 84467 |
| HUGO | 18794 |
| OMIM | 608529 |
| RefSeq | NM_032447 |
| UniProt | Q75N90 |
| Other data | |
| Locus | Chr. 19 p13 |
Fibrillin is a glycoprotein, which is essential for the formation of elastic fibers found in connective tissue.[2] Fibrillin is secreted into the extracellular matrix by fibroblasts and becomes incorporated into the insoluble microfibrils, which appear to provide a scaffold for deposition of elastin.[3]
Contents
Clinical aspect
Mutations in FBN1 and FBN2 are associated with adolescent idiopathic scoliosis .[4]
Types
Fibrillin-1
Fibrillin-1 is a major component of the microfibrils that form a sheath surrounding the amorphous elastin. It is believed that the microfibrils are composed of end-to-end polymers of fibrillin. To date, 3 forms of fibrillin have been described. The fibrillin-1 protein was isolated by Engvall in 1986,[5] and mutations in the FBN1 gene cause Marfan syndrome.[6]
This protein is found in humans, and its genes are found on chromosome 15. At present more than 600 different mutations have been described.[1]
Structure
There is no complete, high-resolution structure of fibrillin-1. Instead, short fragments have been produced recombinantly and their structures solved by X-ray crystallography or using NMR spectroscopy. A recent example is the structure of the fibrillin-1 hybrid2 domain, in context of its flanking calcium binding epidermal growth factor domains, which was determined using X-ray crystallography to a resolution of 1.8 Å.[1] The microfibrils that are made up of fibrillin protein are responsible for different cell-matrix interactions in the human body.
Fibrillin-2
Fibrillin-2 was isolated in 1994 by Zhang[7] and is thought to play a role in early elastogenesis. Mutations in the fibrillin-2 gene have been linked to Beal's Syndrome.
Fibrillin-3
More recently, fibrillin-3 was described and is believed to be located mainly in the brain.[8] Along with the brain, fibrillin-3 has been localized in the gonads and ovaries of field mice.
Fibrillin-4
Fibrillin-4 was first discovered in zebrafish, and has a sequence similar to fibrillin-2.[9]
References
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- Fibrillin at the US National Library of Medicine Medical Subject Headings (MeSH)
- ↑ 1.0 1.1 1.2 PDB: 2W86; Lua error in package.lua at line 80: module 'strict' not found.
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