Sandbox Reserved 820: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 29: | Line 29: | ||
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>. 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+. | <scene name='56/568018/Dimer/8'>α3 helix of the domain I</scene> ( | ||
<scene name='56/568018/Dimer/10'>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+. | |||
<!--Mettre du VERT --> | <!--Mettre du VERT --> | ||
<!-- 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 --> | ||
