DNA binding domain: Difference between revisions
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A [[DNA|DNA]] binding domain is part of a [[Protein|protein]] with a high affinity for DNA. For example, [[Transcription factor|transcription factors]]. | A [[DNA|DNA]] binding domain (DBD) is part of a [[Protein|protein]] with a high affinity for DNA. For example, [[Transcription factor|transcription factors]]. DBDs have a minimum of one [[Motif|motif]] which can bind to non-sequence specific or sequence specific [[DNA|DNA]]. [[Structural motifs|Structural motifs]] can interact with [[Single stranded binding protein|single stranded and]] [[Double helix|double stranded DNA]]. The functions of DBDs include allowing structural changes to take place to a protein and to allow regulation of [[Transcription|transcription]].<ref>L. Swint-Kruse and K. S. Matthews. Curr Opin Microbiol. Allostery in the Lac1/ GalR Family: Variations on a Theme. 2009 Apr; 12(2): 129–137</ref> | ||
Some common examples of DBDs include: | |||
-[[Helix-turn-helix|helix-turn-helix]] | |||
-[[Zinc finger|zinc finger]] | |||
-[[Winged finger|winged helix]] | |||
-[[Helix-loop-helix|helix-loop-helix]], which is present in some [[Transcription factor|transcription factors.]] | |||
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=== References: === | |||
<references /> |
Revision as of 16:58, 1 December 2016
A DNA binding domain (DBD) is part of a protein with a high affinity for DNA. For example, transcription factors. DBDs have a minimum of one motif which can bind to non-sequence specific or sequence specific DNA. Structural motifs can interact with single stranded and double stranded DNA. The functions of DBDs include allowing structural changes to take place to a protein and to allow regulation of transcription.[1]
Some common examples of DBDs include:
-helix-loop-helix, which is present in some transcription factors.
References:
- ↑ L. Swint-Kruse and K. S. Matthews. Curr Opin Microbiol. Allostery in the Lac1/ GalR Family: Variations on a Theme. 2009 Apr; 12(2): 129–137