Sandbox Reserved 1105: Difference between revisions
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At the entry of the binding site, the TTR has a hydrophilic tail, into which the four iodine atoms of the ligand are placed. The dimer interface of the TTR is divided in two part, the inner and the outer binding cavity. The outermost pockets <scene name='82/829358/Hbp1/3'>HBP1</scene> and <scene name='82/829358/Hbp1prim/3'>HBP1'</scene> are located between the side chains of <scene name='82/829358/Hbp1aa/1'>Ala 108, Thr 106, Met 13 and Lys 15</scene> <ref name= "Klabunde">PMID: 10742177</ref>. | At the entry of the binding site, the TTR has a hydrophilic tail, into which the four iodine atoms of the ligand are placed. The dimer interface of the TTR is divided in two part, the inner and the outer binding cavity. The outermost pockets <scene name='82/829358/Hbp1/3'>HBP1</scene> and <scene name='82/829358/Hbp1prim/3'>HBP1'</scene> are located between the side chains of <scene name='82/829358/Hbp1aa/1'>Ala 108, Thr 106, Met 13 and Lys 15</scene> <ref name= "Klabunde">PMID: 10742177</ref>. | ||
The central <scene name='82/829358/Hbp2/2'>HBP2</scene> and <scene name='82/829358/Hbp2prime/1'>HBP2'</scene> are formed by the side chains of Leu 110, Ala 109, Lys 15, and Leu 17, it is primarily hydrophobic with polar or electrostatic contributions from the carbonyl groups of Lys 15, Ala 108 and Ala 109. | The central <scene name='82/829358/Hbp2/2'>HBP2</scene> and <scene name='82/829358/Hbp2prime/1'>HBP2'</scene> are formed by the side chains of <scene name='82/829358/Hbp2aa/1'>Leu 110, Ala 109, Lys 15, and Leu 17</scene>, it is primarily hydrophobic with polar or electrostatic contributions from the carbonyl groups of Lys 15, Ala 108 and Ala 109. | ||
The innermost binding pocket, HBP3, is located between the side chains of | The innermost binding pocket, HBP3, is located between the side chains of Ser 117, Thr 119, Ala 108 and Leu 110. Its surface is composed of aliphatic methyl and methylene groups, as well as the Ser 117 hydroxyl group, the carbonyl groups of Ser 117, Thr 118 and Ala 108, and the main chain NH groups of Thr 119, Ala 109 and Leu 110. | ||