Sandbox Reserved 713: Difference between revisions

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OCA, Andréa Mc Cann

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 <Structure load='2fkl' size='450' align='left' background='none' scene='' caption='[[2fkl]]'/>
-The three dimensional structure of the Cu-Binding Domain was first determined by resonance multidimensional NMR spectroscopy (article DOI 10.1074/jbc. M300629200 –2003). More recently, the determination of the crystallographic structure permits to define the molecular interaction between the Cu-Binding Domain and copper.<ref name="Molecular" />
+The three dimensional structure of the Cu-Binding Domain was first determined by resonance multidimensional NMR spectroscopy <ref name="2003" />. More recently, the determination of the crystallographic structure permits to define the molecular interaction between the Cu-Binding Domain and copper.<ref name="Molecular" />
- <br/>
-fkl is constituted by two chains called A and B<ref> PMID:12611883 </ref>. Both chains have the same length and the same organization. Each chain also contains an <scene name='Sandbox_Reserved_713/Helice_alpha/1'>alpha-helix</scene> going from residue 147 to 159 packed against a triple-strand beta sheet. The strand <scene name='Sandbox_Reserved_719/Beta1/1'>Beta1</scene> going from residue 133 to 139, the <scene name='Sandbox_Reserved_713/Beta_stream2/1'>Beta2</scene> going from residue 162 to 167, and the <scene name='Sandbox_Reserved_713/Beta_stream3/1'>Beta3</scene> going from residue 181 to 188. There is one more Beta sheet, <scene name='Sandbox_Reserved_713/Beta_0/1'>B0</scene>, formed by the residues 127 to 139 of the B chain.
+fkl is constituted by two chains called A and B<ref name="2003"> PMID:12611883 </ref>. Both chains have the same length and the same organization. Each chain also contains an <scene name='Sandbox_Reserved_713/Helice_alpha/1'>alpha-helix</scene> going from residue 147 to 159 packed against a triple-strand beta sheet. The strand <scene name='Sandbox_Reserved_719/Beta1/1'>Beta1</scene> going from residue 133 to 139, the <scene name='Sandbox_Reserved_713/Beta_stream2/1'>Beta2</scene> going from residue 162 to 167, and the <scene name='Sandbox_Reserved_713/Beta_stream3/1'>Beta3</scene> going from residue 181 to 188. There is one more Beta sheet, <scene name='Sandbox_Reserved_713/Beta_0/1'>B0</scene>, formed by the residues 127 to 139 of the B chain.
 Between the Cysteine 133 and the Cystein 187 we can find a <scene name='Sandbox_Reserved_719/Disulfide_bond/1'>disulfide bound</scene>  which links <scene name='Sandbox_Reserved_713/Disulfide_brige_beta1_3/1'>the strand beta 1 and beta 3</scene> and <scene name='Sandbox_Reserved_713/Bislufide_bridge/1'>another one</scene> between cystein 158 and cystein186 which links the alpha helix to the strand Beta 3. Between the cysteine 144 and the cysteine 174 we can describe another <scene name='Sandbox_Reserved_713/Dislfide_brige_2/1'>disulfide bound</scene>.