DNA binding domain: Difference between revisions

From The School of Biomedical Sciences Wiki
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
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)&nbsp;is part of a [[Protein|protein]] with a high affinity for DNA. For example,&nbsp;[[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&nbsp;interact with&nbsp;[[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]],&nbsp;which is&nbsp;present in some [[Transcription factor|transcription factors.]]
 
<br>
 
=== 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-turn-helix

-zinc finger

-winged helix

-helix-loop-helix, which is present in some transcription factors.


References:

  1. 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