Group:MUZIC:Myostatin - Revision history

Jaime Prilusky at 11:31, 1 July 2015

Jaime Prilusky — Wed, 01 Jul 2015 11:31:46 GMT

←Older revision		Revision as of 11:31, 1 July 2015
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	== References ==		== References ==
	<references/>		<references/>
		+	[[Category: Z-disk]]

Michal Harel at 10:04, 18 February 2014

Michal Harel — Tue, 18 Feb 2014 10:04:19 GMT

←Older revision		Revision as of 10:04, 18 February 2014
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	=== Growth/differentiation factor 8 or Myostatin===		=== Growth/differentiation factor 8 or Myostatin===

-	<Structure load='3hh2' size='400' frame='true' align='right' caption='The structure of myostatin:follistatin 288 (PDB ~~3HH2~~)' scene='Group:MUZIC:Myostatin/Myostatin/1'/>	+	<Structure load='3hh2' size='400' frame='true' align='right' caption='The structure of myostatin:follistatin 288 (PDB [[3hh2]])' scene='Group:MUZIC:Myostatin/Myostatin/1'/>

Michal Harel at 10:30, 7 July 2013

Michal Harel — Sun, 07 Jul 2013 10:30:56 GMT

←Older revision		Revision as of 10:30, 7 July 2013
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	== Introduction ==		== Introduction ==

-	Myostatin which is also known as '''growth/differentiation factor-8 (GDF-8)''' was originally identified in a screen for novel mammalian members of the transforming growth factor-ß (TGF-ß) superfamily of growth and differentiation factors.The phenotype of myostatin knock-out mice suggested that myostatin functions as a negative regulator of muscle growth, and it was on this basis that myostatin was given its name <ref>PMID:9139826</ref>. For these reasons, inhibitors targeting myostatin have been regarded as potential drugs in the treatment of muscle-wasting disorders such as muscular dystrophy <ref>PMID: 18425412 </ref>.	+	'''Myostatin''' which is also known as '''growth/differentiation factor-8 (GDF-8)''' was originally identified in a screen for novel mammalian members of the transforming growth factor-ß (TGF-ß) superfamily of growth and differentiation factors.The phenotype of myostatin knock-out mice suggested that myostatin functions as a negative regulator of muscle growth, and it was on this basis that myostatin was given its name <ref>PMID:9139826</ref>. For these reasons, inhibitors targeting myostatin have been regarded as potential drugs in the treatment of muscle-wasting disorders such as muscular dystrophy <ref>PMID: 18425412 </ref>.

	== Sequence annotation ==		== Sequence annotation ==

Nikos Pinotsis at 11:48, 2 April 2013

Nikos Pinotsis — Tue, 02 Apr 2013 11:48:40 GMT

←Older revision		Revision as of 11:48, 2 April 2013
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		+	=== Growth/differentiation factor 8 or Myostatin===
		+
	<Structure load='3hh2' size='400' frame='true' align='right' caption='The structure of myostatin:follistatin 288 (PDB 3HH2)' scene='Group:MUZIC:Myostatin/Myostatin/1'/>		<Structure load='3hh2' size='400' frame='true' align='right' caption='The structure of myostatin:follistatin 288 (PDB 3HH2)' scene='Group:MUZIC:Myostatin/Myostatin/1'/>

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	== Introduction ==		== Introduction ==

-	Myostatin which is also known as growth ~~and developmental~~ factor-8(GDF-8) was originally identified in a screen for novel mammalian members of the transforming growth factor-ß (TGF-ß) superfamily of growth and differentiation factors.The phenotype of myostatin knock-out mice suggested that myostatin functions as a negative regulator of muscle growth, and it was on this basis that myostatin was given its name <ref>PMID:9139826</ref>. For these reasons, inhibitors targeting myostatin have been regarded as potential drugs in the treatment of muscle-wasting disorders such as muscular dystrophy <ref>PMID: 18425412 </ref>.	+	Myostatin which is also known as '''growth/differentiation factor-8 (GDF-8)''' was originally identified in a screen for novel mammalian members of the transforming growth factor-ß (TGF-ß) superfamily of growth and differentiation factors.The phenotype of myostatin knock-out mice suggested that myostatin functions as a negative regulator of muscle growth, and it was on this basis that myostatin was given its name <ref>PMID:9139826</ref>. For these reasons, inhibitors targeting myostatin have been regarded as potential drugs in the treatment of muscle-wasting disorders such as muscular dystrophy <ref>PMID: 18425412 </ref>.

	== Sequence annotation ==		== Sequence annotation ==
-	Myostatin ~~consists~~ of three functional fragments: signal peptide, N-terminal and C-terminal fragments. Amino acid sequences among vertebrate species are highly conserved, which also suggests the conserved function of myostatin among vertebrates <ref>PMID: 9356471 </ref>.	+	Myostatin is a 375 amino-acid protein consisting of three functional fragments [http://www.uniprot.org/uniprot/O14793 (Uniprot:O14793)]: signal peptide, N-terminal and C-terminal fragments. Amino acid sequences among vertebrate species are highly conserved, which also suggests the conserved function of myostatin among vertebrates <ref>PMID: 9356471 </ref>.

	[[Image:myostatin.jpg]]		[[Image:myostatin.jpg]]

Jae-Geun Song: /* Structure */

Jae-Geun Song — Mon, 11 Feb 2013 11:27:12 GMT

Structure

←Older revision		Revision as of 11:27, 11 February 2013
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	== Structure ==		== Structure ==
-	The complex of two follistatin 288 molecules bound to one myostatin dimer was resolved to 2.15 Å using X-ray crystallography and deposited in PDB. Myostatin shows a typical hand-shaped structure of TGF-beta family. When myostatin binds to Fst288, which increase the affinity to heparin due to the basic ~~surfece~~ of the complex <ref>PMID: 19644449</ref>.	+	The complex of two follistatin 288 molecules bound to one myostatin dimer was resolved to 2.15 Å using X-ray crystallography and deposited in PDB. Myostatin shows a typical hand-shaped structure of TGF-beta family. When myostatin binds to Fst288, which increase the affinity to heparin due to the continuous basic surface of the complex <ref>PMID: 19644449</ref>.
	(Green:myostatin C-terminal dimer, yellow: follinstatin 288)		(Green:myostatin C-terminal dimer, yellow: follinstatin 288)

Jae-Geun Song: /* Structure */

Jae-Geun Song — Mon, 11 Feb 2013 11:26:29 GMT

Structure

←Older revision		Revision as of 11:26, 11 February 2013
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	== Structure ==		== Structure ==
-	~~One structure of myostatin is currently available in Protein Data Bank.~~	+	The complex of two follistatin 288 molecules bound to one myostatin dimer was resolved to 2.15 Å using X-ray crystallography and deposited in PDB. Myostatin shows a typical hand-shaped structure of TGF-beta family. When myostatin binds to Fst288, which increase the affinity to heparin due to the basic surfece of the complex <ref>PMID: 19644449</ref>.
-	The complex of two follistatin 288 molecules bound to one myostatin dimer was resolved to 2.15 Å using X-ray crystallography and deposited in PDB.	+
	(Green:myostatin C-terminal dimer, yellow: follinstatin 288)		(Green:myostatin C-terminal dimer, yellow: follinstatin 288)

Jae-Geun Song: /* Sequence annotation */

Jae-Geun Song — Mon, 11 Feb 2013 11:14:57 GMT

Sequence annotation

←Older revision		Revision as of 11:14, 11 February 2013
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	== Sequence annotation ==		== Sequence annotation ==
	Myostatin consists of three functional fragments: signal peptide, N-terminal and C-terminal fragments. Amino acid sequences among vertebrate species are highly conserved, which also suggests the conserved function of myostatin among vertebrates <ref>PMID: 9356471 </ref>.		Myostatin consists of three functional fragments: signal peptide, N-terminal and C-terminal fragments. Amino acid sequences among vertebrate species are highly conserved, which also suggests the conserved function of myostatin among vertebrates <ref>PMID: 9356471 </ref>.
		+
	[[Image:myostatin.jpg]]		[[Image:myostatin.jpg]]

Jae-Geun Song: /* Sequence annotation */

Jae-Geun Song — Mon, 11 Feb 2013 11:14:45 GMT

Sequence annotation

←Older revision		Revision as of 11:14, 11 February 2013
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	== Sequence annotation ==		== Sequence annotation ==
	Myostatin consists of three functional fragments: signal peptide, N-terminal and C-terminal fragments. Amino acid sequences among vertebrate species are highly conserved, which also suggests the conserved function of myostatin among vertebrates <ref>PMID: 9356471 </ref>.		Myostatin consists of three functional fragments: signal peptide, N-terminal and C-terminal fragments. Amino acid sequences among vertebrate species are highly conserved, which also suggests the conserved function of myostatin among vertebrates <ref>PMID: 9356471 </ref>.
-	[[Image:myostatin.jpg]]	+	[[Image:myostatin.jpg]]

	== Structure ==		== Structure ==

Jae-Geun Song at 11:14, 11 February 2013

Jae-Geun Song — Mon, 11 Feb 2013 11:14:17 GMT

←Older revision		Revision as of 11:14, 11 February 2013
Line 8:		Line 8:
	== Sequence annotation ==		== Sequence annotation ==
	Myostatin consists of three functional fragments: signal peptide, N-terminal and C-terminal fragments. Amino acid sequences among vertebrate species are highly conserved, which also suggests the conserved function of myostatin among vertebrates <ref>PMID: 9356471 </ref>.		Myostatin consists of three functional fragments: signal peptide, N-terminal and C-terminal fragments. Amino acid sequences among vertebrate species are highly conserved, which also suggests the conserved function of myostatin among vertebrates <ref>PMID: 9356471 </ref>.
-
	[[Image:myostatin.jpg]]		[[Image:myostatin.jpg]]

Jae-Geun Song: /* Sequence annotation */

Jae-Geun Song — Mon, 11 Feb 2013 11:13:58 GMT

Sequence annotation

←Older revision		Revision as of 11:13, 11 February 2013
Line 7:		Line 7:

	== Sequence annotation ==		== Sequence annotation ==
-	Myostatin consists of three functional fragments: signal peptide, N-terminal and C-terminal fragments. Amino acid sequences among vertebrate species are highly conserved, which also suggests the conserved function of myostatin among vertebrates. [[Image:myostatin.jpg]]	+	Myostatin consists of three functional fragments: signal peptide, N-terminal and C-terminal fragments. Amino acid sequences among vertebrate species are highly conserved, which also suggests the conserved function of myostatin among vertebrates <ref>PMID: 9356471 </ref>.
		+
		+	[[Image:myostatin.jpg]]

	== Structure ==		== Structure ==