Sandbox Reserved 433: Difference between revisions
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It is observed that there are direct H-bonds, water-mediated polar interactions and hydrophobic interactions in the GSK-3β and staurosporine complex. | It is observed that there are direct H-bonds, water-mediated polar interactions and hydrophobic interactions in the GSK-3β and staurosporine complex. | ||
There are only two direct H-bonds, and they are observed between | There are only two direct H-bonds, and they are observed between | ||
* The <span style="color:red">'''carbonyl oxygen'''</span> of Asp 133 and <span style="color:blue">'''N<sup>1</sup> (nitrogen)'''</span> of staurosporine. The length of this hydrogen bond is 2.93 Å. | |||
* The backbone <span style="color:blue">'''nitrogen'''</span> of Val 135 and <span style="color:red">'''O<sup>5</sup> (oxygen)'''</span> of staurosporine. The length of this hydrogen bond is 2.76 Å. | |||
Besides direct H-bond, the water-mediated polar interactions are observed between the <span style="color:red">'''carbonyl oxygen'''</span> of Gln 185 and <span style="color:blue">'''N<sup>4</sup> (nitrogen)'''</span> of the glycosidic ring. | Besides direct H-bond, the water-mediated polar interactions are observed between the <span style="color:red">'''carbonyl oxygen'''</span> of Gln 185 and <span style="color:blue">'''N<sup>4</sup> (nitrogen)'''</span> of the glycosidic ring. | ||
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However, the length between between Gln 185 and Strauroporine is 4.47 Å which surpasses typical H-bond distance; therefore, it forms a water mediated polar interaction between these atoms instead of direct H-bond [cite J,A,Bertrand] | However, the length between between Gln 185 and Strauroporine is 4.47 Å which surpasses typical H-bond distance; therefore, it forms a water mediated polar interaction between these atoms instead of direct H-bond [cite J,A,Bertrand] | ||
This is a unique interaction to the GSK-3β and staurosporine complex, since other protein kinase (e.g. CDK2, Chk1, LCK, PKA) -staurosporine complexes show direct H-bond interaction between two moieties. | This is a unique interaction to the GSK-3β and staurosporine complex, since other protein kinase (e.g. CDK2, Chk1, LCK, PKA) -staurosporine complexes show direct H-bond interaction between two moieties. | ||
There is a significant number of <scene name='48/483890/Additional_feature_v4/2'>hydrophobic interaction</scene> in the GSK-3β and staurosporine complex; to be more specific, this complex buries 891 Å<sup>2</sup> surface area [cite J,A,Bertrand]. | There is a significant number of <scene name='48/483890/Additional_feature_v4/2'>hydrophobic interaction</scene> in the GSK-3β and staurosporine complex; to be more specific, this complex buries 891 Å<sup>2</sup> surface area [cite J,A,Bertrand]. | ||
