Sandbox Mati
From Proteopedia
(Difference between revisions)
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Two <scene name='43/437742/2yxj_hydrophobic/2'>hydrophobic patches</scene> which include Phe191 Val141 and | Two <scene name='43/437742/2yxj_hydrophobic/2'>hydrophobic patches</scene> which include Phe191 Val141 and | ||
Ala93 for one, and the other patch includes Phe146 Val126 and Leu108. A look at the <scene name='43/437742/2yxj_space_fill_color_charged/3'>Overall</scene> picture shows that there are hydrophobic patches (in gray) "above" and "below" the ligand ,negatively charged residues "above-right" and "below-left" of the ligand and positively charges on the "right" and "left" of it. | Ala93 for one, and the other patch includes Phe146 Val126 and Leu108. A look at the <scene name='43/437742/2yxj_space_fill_color_charged/3'>Overall</scene> picture shows that there are hydrophobic patches (in gray) "above" and "below" the ligand ,negatively charged residues "above-right" and "below-left" of the ligand and positively charges on the "right" and "left" of it. | ||
| - | This symmetry can be exploited, a symmetric molecule can bind the same interface in two different ways thus increasing the "chance" of binding which means better binding affinity. | + | This symmetry can be exploited, a symmetric molecule can bind the same interface in two different ways thus increasing the "chance" of binding which means better binding affinity.> |
Revision as of 12:24, 1 September 2013
Symmetry in the Bcl-Xl interface
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