Sandbox Reserved 820: Difference between revisions
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<scene name='56/568018/Oligomere_and_ligand/3'>homooligomers</scene>. | <scene name='56/568018/Oligomere_and_ligand/3'>homooligomers</scene>. | ||
There are two types of dimerisation: the | There are two types of dimerisation: the | ||
<scene name='56/568018/Dimer/1'>front-to-front form</scene> and the <scene name='56/568018/Oligomere_and_ligand/ | <scene name='56/568018/Dimer/1'>front-to-front form</scene> and the <scene name='56/568018/Oligomere_and_ligand/5'>back-to-back form</scene>. <ref name="Crystal Structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum (Wang et al., 1998)">Crystal Structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum (Wang et al., 1998) http://www.nature.com/nsmb/journal/v5/n6/abs/nsb0698-476.html</ref> | ||
The front-to-front form is stabilized by intermolecular interactions between the | The front-to-front form is stabilized by intermolecular interactions between the | ||
<scene name='56/568018/Dimer/3'>α2 helix of the domain I</scene> of each CASQ2.<ref name="Crystal Structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum (Wang et al., 1998)">http://www.nature.com/nsmb/journal/v5/n6/abs/nsb0698-476.html</ref> The intermolecular salt bridges are built between <scene name='56/568018/Dimer/13'>Glu 55 and Lys 49</scene>.<ref name="Crystal Structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum (Wang et al., 1998)">http://www.nature.com/nsmb/journal/v5/n6/abs/nsb0698-476.html</ref>This dimerisation induces the formation of an electronegative pocket which involves these amino acids: for the first CASQ2 Glu 39, Glu 54, Glu 78, Glu 92, Asp 93 and Asp 101 and for the second CASQ2 Glu 199, Asp 245, Asp 278, Glu 350 and Glu 348.<ref name="Crystal Structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum (Wang et al., 1998)">http://www.nature.com/nsmb/journal/v5/n6/abs/nsb0698-476.html</ref> <!--Mettre du VERT --> | <scene name='56/568018/Dimer/3'>α2 helix of the domain I</scene> of each CASQ2.<ref name="Crystal Structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum (Wang et al., 1998)">http://www.nature.com/nsmb/journal/v5/n6/abs/nsb0698-476.html</ref> The intermolecular salt bridges are built between <scene name='56/568018/Dimer/13'>Glu 55 and Lys 49</scene>.<ref name="Crystal Structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum (Wang et al., 1998)">http://www.nature.com/nsmb/journal/v5/n6/abs/nsb0698-476.html</ref>This dimerisation induces the formation of an electronegative pocket which involves these amino acids: for the first CASQ2 Glu 39, Glu 54, Glu 78, Glu 92, Asp 93 and Asp 101 and for the second CASQ2 Glu 199, Asp 245, Asp 278, Glu 350 and Glu 348.<ref name="Crystal Structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum (Wang et al., 1998)">http://www.nature.com/nsmb/journal/v5/n6/abs/nsb0698-476.html</ref> <!--Mettre du VERT --> | ||
