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OCA, Marc-Antoine Jaques, Thomas Vuillemin, Stéphanie Gross

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	<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 dimerization induces the formation of an electronegative pocket which involves the following amino acids: Glu 39, Glu 54, Glu 78, Glu 92, Asp 93 and Asp 101 for the first monomere and Glu 199, Asp 245, Asp 278, Glu 348 and Glu 350 for the second one.<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>		<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 dimerization induces the formation of an electronegative pocket which involves the following amino acids: Glu 39, Glu 54, Glu 78, Glu 92, Asp 93 and Asp 101 for the first monomere and Glu 199, Asp 245, Asp 278, Glu 348 and Glu 350 for the second one.<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 back-to-back form is stabilized by intermolecular interactions between the <scene name='56/568018/Oligomere_and_ligand/7'>α3 helix of the domain I</scene>, <scene name='56/568018/Oligomere_and_ligand/6'>α4 helix of the domain II</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>, and it has also been proved that the <scene name='56/568018/Oligomere_and_ligand/18'>C-term domain</scene> is involved<ref name="c term">NCBI Structure Ressource: CASQ2 calsequestrin 2 http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi</ref> (<scene name='56/568018/Oligomere_and_ligand/9'>together</scene>). The intermolecular salt bridges are built between Glu 215 and Lys 86, Glu 216 and Lys 24, Glu 169 and Lys 85.<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 dimerization is also favored by a hydrogen bond between Ala 82 and Asn 22. This dimerization creates a very electronegative pocket at the C-terminal region which enables the binding of Ca<sup>2+</sup>.<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 back-to-back form is stabilized by intermolecular interactions between the <scene name='56/568018/Oligomere_and_ligand/7'>α3 helix of the domain I</scene>, <scene name='56/568018/Oligomere_and_ligand/6'>α4 helix of the domain II</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>, and it has also been proved that the <scene name='56/568018/Oligomere_and_ligand/18'>C-term domain</scene> is involved<ref name="c term">NCBI Structure Ressource: CASQ2 calsequestrin 2 http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi</ref> (<scene name='56/568018/Oligomere_and_ligand/9'>all together</scene>). The intermolecular salt bridges are built between Glu 215 and Lys 86, Glu 216 and Lys 24, Glu 169 and Lys 85.<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 dimerization is also favored by a hydrogen bond between Ala 82 and Asn 22. This dimerization creates a very electronegative pocket at the C-terminal region which enables the binding of Ca<sup>2+</sup>.<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>