DNA-protein interactions

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<StructureSection load='1d66' size='340' side='right' caption='Gal4 transcriptional activator interacting with its target DNA=''>
<StructureSection load='1d66' size='340' side='right' caption='Gal4 transcriptional activator interacting with its target DNA=''>
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While DNA contains all the genetic material in a cell, proteins play an important role in regulating the transcription of DNA to RNA, not to mention replication, repair and packaging.. The interactions between [[DNA]] and proteins are important in this process. Most sequence specific interactions occur in the major grove, as portions of the bases are exposed in this groove. In contrast, the minor groove contains more of the carbohydrate portions of DNA.
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While DNA contains all the genetic material in a cell, proteins play an important role in regulating the transcription of DNA to RNA, not to mention replication, repair and packaging.. The interactions between [[DNA]] and proteins are important in this process. Most sequence specific interactions occur in the <scene name='71/711660/Grooves/1'>major grove</scene>, as the <scene name='71/711660/Base_exposure/1'>bases are exposed</scene> in this groove. In contrast, the <scene name='71/711660/Grooves/1'>minor grove</scene> contains more of the <scene name='71/711660/Base_exposure/1'>carbohydrate portions</scene> of DNA.
== Helix-Turn-Helix Interactions with DNA==
== Helix-Turn-Helix Interactions with DNA==
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The first DNA binding domain characterized was the helix-turn-helix. In helix-turn-helix protein, two α helices are joined by a turn. In most cases, such as in the Cro repressor, the C terminal helix contributes most to DNA recognition, and hence it is often called the "recognition helix". It binds to the major groove of DNA through a series of hydrogen bonds and various Van der Waals interactions with exposed bases.The N-terminal alpha helix stabilizes the interaction between the interaction between protein and DNA, but does not play a particularly strong role in its recognition.[2] The recognition helix and its preceding helix always have the same relative orientation.[
== Leucine zippers ==
== Leucine zippers ==

Revision as of 23:02, 2 September 2015

DNA-Protein interactions

PDB ID 1d66

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References

This text shows how to insert references: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Proteopedia Page Contributors and Editors (what is this?)

Ann Taylor, Eric Martz, Michal Harel

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