Sandbox Reserved 426
| This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
Structure of Oligonucleotide/Drug complex (1xcs)
by Michael Beauregard, Annie Burton, Jianlong Li, Daniel Marco, and Nathaneal Park
Introduction
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This scene shows the two main strands in this protein. Notice the similarity in shape and side chains.
Everyone -- note that this is NOT a protein, but a complex with DNA. Edit your text accordingly, eg discussing alpha helices etc does not make sense.
Overall Structure
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The 1xcs (model at right) protein is a small, simple globular protein lacking any clear secondary beta sheets or alpha helices. The protein consists of two non-identical dimers. A simplified model of 1xcs is shown here, with the side chains removed for clarity. The protein can be followed from N to C terminus following along each strand from blue to red. Note that the strands are antiparallel where they are non-covalently bound. 1xcs with the side chains displayed (black) visualizes this bonding in the middle region of the protein, again following each strand from blue to red from N to C terminus.
Binding Interactions
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Additional Features
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Click here to see that the protein binds directly between strands of DNA. This interrupts the expression of this section of DNA.
Quiz Question 1
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Why is it important for the protein to bind here?
A unique site is the __ ion found associated with the O6_atom_of_two_guanines, which gives additional strength to the guanine–Co2+–guanine interaction. A Mg2+ B Co2+ C Ba2+ D Mg2+
See Also
Credits
Introduction - Daniel Marco
Overall Structure - Nathaneal Park
Drug Binding Site - Annie Burton
Additional Features - Michael Beauregard
Quiz Question 1 - Jianlong Li
