Sandbox Reserved 820: Difference between revisions
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The back-to-back form is stabilized by intermolecular interactions between the <scene name='56/568018/Dimer/9'>α4 helix of the domain II</scene> and the | The back-to-back form is stabilized by intermolecular interactions between the <scene name='56/568018/Dimer/9'>α4 helix of the domain II</scene> and the | ||
<scene name='56/568018/Dimer/8'>α3 helix of the domain I</scene> ( | <scene name='56/568018/Dimer/8'>α3 helix of the domain I</scene> ( | ||
<scene name='56/568018/Dimer/ | <scene name='56/568018/Dimer/11'>together</scene>). The intermolecular salt bridges are between Glu 215 and Lys 86, Glu 216 and Lys 24, Glu 169 and Lys 85. There is also a hydrogen bond between Ala 82 and Asn 22. This dimerisation induces a very electronegative pocket at the C-terminal region which enables the binding of Ca2+. | ||
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<!-- Source: Crystal Structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum (Wang et al., 1998) Lien: http://www.nature.com/nsmb/journal/v5/n6/abs/nsb0698-476.html --> | <!-- Source: Crystal Structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum (Wang et al., 1998) Lien: http://www.nature.com/nsmb/journal/v5/n6/abs/nsb0698-476.html --> | ||
