Sandbox Reserved 1092: Difference between revisions

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= Structure and synthesis <ref name="Structure and synthesis"> Université de Montpellier. Physiologie expérimentale du coeur et des muscles : la myostatine/partenaires de la myostatine. [https://u1046.edu.umontpellier.fr/163-2/abrege-des-proteines-musculaires/myostatine/]</ref> =  
= Structure and synthesis <ref name="Structure and synthesis"> Université de Montpellier. Physiologie expérimentale du coeur et des muscles : la myostatine/partenaires de la myostatine. [https://u1046.edu.umontpellier.fr/163-2/abrege-des-proteines-musculaires/myostatine/]</ref> =  
== Primary and secondary structures ==
== Primary and secondary structures ==
Myostatin is a '''42,7 kDa''' protein composed of only 108 residues in its mature form. It contains 7 <scene name='82/829345/Cys/5'>cystein</scene>  residues in its C-terminal domain, all of which are involved in '''disulfide bridges'''. The secondary structure of myostatin is composed of two strands, both made of<scene name='82/829345/Sheets/1'>short antiparallel structures</scene>. The structure is also made of '''3 alpha helices''' :  
Myostatin is a '''42,7 kDa''' protein composed of only 108 residues in its mature form. It contains 7 <scene name='82/829345/Cys/5'>cystein</scene>  residues in its C-terminal domain, all of which are involved in '''disulfide bridges'''. The secondary structure of myostatin is composed of two strands, both made of short <scene name='82/829345/Sheets/1'> antiparallel structures</scene>. The structure is also made of 3 <scene name='82/829345/Helices/2'>α helices </scene> :  


- '''Helix alpha-1''' : containing between 4 and 7 residues (non-visible on the structure)
- '''Helix α-1''' : containing between 4 and 7 residues (non-visible on the structure)


- '''Helix alpha-2''' : containing between 24 and 28 residues  
- '''Helix α-2''' : containing between 24 and 28 residues  


- '''Helix alpha-3''' : containing between 58 and 68 residues
- '''Helix α-3''' : containing between 58 and 68 residues


The folding of these structures gives myostatin a slightly bent, hand-like shape, with 2 fingers formed by the strands described above. The palm of the hand is formed by the helix alpha-3. The N- and C-terminal ends are situated very close to the palm and the last 10 residues on the N-terminal side form the thumb of the hand.  
The folding of these structures gives myostatin a slightly bent, hand-like shape, with 2 fingers formed by the strands described above. The palm of the hand is formed by the helix alpha-3. The N- and C-terminal ends are situated very close to the palm and the last 10 residues on the N-terminal side form the thumb of the hand.