Sandbox Reserved 1493: Difference between revisions

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Its <scene name='80/802667/Beta_head/2'>head</scene> is composed of a '''β I domain''' which has a fold similar to the I domain of the head of the α subunit. Is has a <scene name='80/802667/Mg_in_beta_head_midas/2'>Mg2+</scene> coordinating '''metal ion dependent adhesion site (MIDAS)''' motif and a site adjacent to MIDAS ('''ADMIDAS''') which coordinates ions and plays a part in activity modulation. In the head can be found the RGD and KGD binding sites.

Its '''stalk''' is mainly composed of a plexin-sempahorin-integrin (PSI) domain and a '''hybrid domain'''. A <scene name='80/802667/Beta_head_cysteines_core/1'>cysteine-rich core</scene> ''(Cys displayed in purple, disulfide bonds in yellow)'' occupies the stalk of β3 from residues 400 to 650. Other cysteins ~~links~~ the N-terminal of the protein to the β I domain thanks to a long-range disulfide bond. <scene name='80/802667/Beta_head_cysteines/1'>Cysteines</scene> of the extracellular domain of the β subunit are thought to have a role in the activation of the headpiece.

Its '''stalk''' is mainly composed of a plexin-sempahorin-integrin (PSI) domain and a '''hybrid domain'''. A <scene name='80/802667/Beta_head_cysteines_core/1'>cysteine-rich core</scene> ''(Cys displayed in purple, disulfide bonds in yellow)'' occupies the stalk of β3 from residues 400 to 650. Other cysteins link the N-terminal of the protein to the β I domain thanks to a long-range disulfide bond. <scene name='80/802667/Beta_head_cysteines/1'>Cysteines</scene> of the extracellular domain of the β subunit are thought to have a role in the activation of the headpiece.

The cytoplasmic tail of the β3 subunit has a NPLY domain which binds proteins with phosphotyrosine binding (PTB) domains.

Sandbox Reserved 1493: Difference between revisions

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@@ Line 37: / Line 37: @@
 Its <scene name='80/802667/Beta_head/2'>head</scene> is composed of a '''β I domain''' which has a fold similar to the I domain of the head of the α subunit. Is has a <scene name='80/802667/Mg_in_beta_head_midas/2'>Mg2+</scene> coordinating '''metal ion dependent adhesion site (MIDAS)''' motif and a site adjacent to MIDAS ('''ADMIDAS''') which coordinates ions and plays a part in activity modulation. In the head can be found the RGD and KGD binding sites.
-Its '''stalk''' is mainly composed of a plexin-sempahorin-integrin (PSI) domain and a '''hybrid domain'''. A <scene name='80/802667/Beta_head_cysteines_core/1'>cysteine-rich core</scene> ''(Cys displayed in purple, disulfide bonds in yellow)'' occupies the stalk of β3 from residues 400 to 650. Other cysteins links the N-terminal of the protein to the β I domain thanks to a long-range disulfide bond. <scene name='80/802667/Beta_head_cysteines/1'>Cysteines</scene> of the extracellular domain of the β subunit are thought to have a role in the activation of the headpiece.
+Its '''stalk''' is mainly composed of a plexin-sempahorin-integrin (PSI) domain and a '''hybrid domain'''. A <scene name='80/802667/Beta_head_cysteines_core/1'>cysteine-rich core</scene> ''(Cys displayed in purple, disulfide bonds in yellow)'' occupies the stalk of β3 from residues 400 to 650. Other cysteins link the N-terminal of the protein to the β I domain thanks to a long-range disulfide bond. <scene name='80/802667/Beta_head_cysteines/1'>Cysteines</scene> of the extracellular domain of the β subunit are thought to have a role in the activation of the headpiece.
 The cytoplasmic tail of the β3 subunit has a NPLY domain which binds proteins with phosphotyrosine binding (PTB) domains.