Sandbox Reserved 1645: Difference between revisions

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The protein fibrillin-1 contains 59 subunits either called '''epidermal growth factor-like domain''' ([[EGF]]), or '''transforming growth factor β binding protein-like domain''' (8 TGF-bp). EGFs are repeated in tandem along with the whole protein which represents about 75% of the total Fibrillin-1 length, and they are interrupted by the insertion of the TGF-bp units, which contain 8 cysteines each which form <scene name='86/868178/Disulfide_bridges_in_tgf-bp/2'>4 disulfide bridges</scene>. In total, there are 47 motifs of EGF in one Fibrillin-1, but only 43 of them contain calcium-binding sequences. In consequence, these EGF are named cb-EGF for their ability to bind calcium cations. Each EGF or cb-EGF unit contains 6 residues of cysteine which form <scene name='86/868178/Disulfide_bridges/1'>3 disulfide bridges</scene> (CYS1-CYS3, CYS2-CYS4, CYS5-CYS6) stabilizing the secondary structure of the protein. Cb-EGF units contain also a <scene name='86/868178/Ca_binding_site/1'>Ca2+ binding site</scene> composed especially of amino acids that contain an oxygen atom, or groups with an azote in their lateral chains (aspartic and glutamic acids, serine, asparagine and glutamine). These amino acids stabilize the calcium cation by interactions between positively charged cation and hetero-atoms (oxygen or azote) of the amino acid's lateral chain. Consequently, a pentagonal bipyramidal binding site is created in which one calcium cation is bound in every cb-EGF subunit of the fibrillin-1 protein. <ref>Sandra Schrenk Carola Cenzi Thomas Bertalot Maria Teresa Conconi Rosa Di Liddo, (2017), pages: 1213-1223,https://doi.org/10.3892/ijmm.2017.3343</ref>
The protein fibrillin-1 contains 59 subunits either called '''epidermal growth factor-like domain''' ([[EGF]]), or '''transforming growth factor β binding protein-like domain''' (8 TGF-bp). EGFs are repeated in tandem along with the whole protein which represents about 75% of the total Fibrillin-1 length, and they are interrupted by the insertion of the TGF-bp units, which contain 8 cysteines each which form <scene name='86/868178/Disulfide_bridges_in_tgf-bp/2'>4 disulfide bridges</scene>. In total, there are 47 motifs of EGF in one Fibrillin-1, but only 43 of them contain calcium-binding sequences. In consequence, these EGF are named cb-EGF for their ability to bind calcium cations. Each EGF or cb-EGF unit contains 6 residues of cysteine which form <scene name='86/868178/Disulfide_bridges/1'>3 disulfide bridges</scene> (CYS1-CYS3, CYS2-CYS4, CYS5-CYS6) stabilizing the secondary structure of the protein. Cb-EGF units contain also a <scene name='86/868178/Ca_binding_site/1'>Ca2+ binding site</scene> composed especially of amino acids that contain an oxygen atom, or groups with an azote in their lateral chains (aspartic and glutamic acids, serine, asparagine and glutamine). These amino acids stabilize the calcium cation by interactions between positively charged cation and hetero-atoms (oxygen or azote) of the amino acid's lateral chain. Consequently, a pentagonal bipyramidal binding site is created in which one calcium cation is bound in every cb-EGF subunit of the fibrillin-1 protein. <ref>Sandra Schrenk Carola Cenzi Thomas Bertalot Maria Teresa Conconi Rosa Di Liddo, (2017), pages: 1213-1223,https://doi.org/10.3892/ijmm.2017.3343</ref>
== FBN1 gene ==
This gene encodes a member of the fibrillin family of proteins. The encoded preproprotein is proteolytically processed to generate two proteins including the extracellular matrix component fibrillin-1 and the protein hormone asprosin. Fibrillin-1 is an extracellular matrix glycoprotein that serves as a structural component of calcium-binding microfibrils. These microfibrils provide force-bearing structural support in elastic and nonelastic connective tissue throughout the body. Asprosin, secreted by white adipose tissue, has been shown to regulate glucose homeostasis. Mutations in this gene are associated with Marfan syndrome and the related MASS phenotype, as well as ectopia lentis syndrome, Weill-Marchesani syndrome, Shprintzen-Goldberg syndrome and neonatal progeroid syndrome. [provided by RefSeq, Apr 2016]




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The FBN-1 gene is involved in a variety of embryonic developmental programs. The microfibrils that are made from fibrillin-1 contribute to both elastic and non-elastic structures. The formation of the elastic fibers in the heart valves and the aorta require the involvement of both FBN-1 and FBN-2.It has been shown that both FBN-1 and FBN-2, along with the other components of elastic fibers, are expressed in the embryonic semilunar valves as early as 4 weeks of gestation. These molecules interact to form the elastic fibers in the ventricularis layer of the semilunar valves. Fibrillin-1 and fibrillin-2 are also crucial for the development of elastic fibers in the aorta. While expression of fibrillin-2 decreases significantly after fetal development, the expression of fibrillin-1 continues into adulthood. This supports the idea that fibrilin-2 dictates the development of early elastic fibers, while fibrillin-1 provides the structural support of mature elastic fibers.
The FBN-1 gene is involved in a variety of embryonic developmental programs. The microfibrils that are made from fibrillin-1 contribute to both elastic and non-elastic structures. The formation of the elastic fibers in the heart valves and the aorta require the involvement of both FBN-1 and FBN-2.It has been shown that both FBN-1 and FBN-2, along with the other components of elastic fibers, are expressed in the embryonic semilunar valves as early as 4 weeks of gestation. These molecules interact to form the elastic fibers in the ventricularis layer of the semilunar valves. Fibrillin-1 and fibrillin-2 are also crucial for the development of elastic fibers in the aorta. While expression of fibrillin-2 decreases significantly after fetal development, the expression of fibrillin-1 continues into adulthood. This supports the idea that fibrilin-2 dictates the development of early elastic fibers, while fibrillin-1 provides the structural support of mature elastic fibers.
== FBN1 gene ==
This gene encodes a member of the fibrillin family of proteins. The encoded preproprotein is proteolytically processed to generate two proteins including the extracellular matrix component fibrillin-1 and the protein hormone asprosin. Fibrillin-1 is an extracellular matrix glycoprotein that serves as a structural component of calcium-binding microfibrils. These microfibrils provide force-bearing structural support in elastic and nonelastic connective tissue throughout the body. Asprosin, secreted by white adipose tissue, has been shown to regulate glucose homeostasis. Mutations in this gene are associated with Marfan syndrome and the related MASS phenotype, as well as ectopia lentis syndrome, Weill-Marchesani syndrome, Shprintzen-Goldberg syndrome and neonatal progeroid syndrome. [provided by RefSeq, Apr 2016]


== Diseases caused by mutation ==
== Diseases caused by mutation ==
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