Sandbox Reserved 820: Difference between revisions
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There are two types of dimerisation: the front-to-front form and the back-to-back form. | There are two types of dimerisation: the front-to-front form and the back-to-back form. | ||
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. The intermolecular salt bridges are built between <scene name='56/568018/Dimer/ | <scene name='56/568018/Dimer/3'>α2 helix of the domain I</scene> of each CASQ2. The intermolecular salt bridges are built between <scene name='56/568018/Dimer/13'>Glu 55 and Lys 49</scene>. 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. <!--Mettre du VERT --> | ||
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 | ||
