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Recombination-activating gene: Difference between revisions

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==Recombination Activating Gene Complex==
==Recombination-Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='RAG1 (grey, pink) and RAG2 (green, yellow) complex with DNA and Zn+2 (grey) (PDB code [[3jbw]])'>
<StructureSection load='3jbw' size='340' side='right' caption='RAG1 (grey, pink) and RAG2 (green, yellow) complex with DNA and Zn+2 (grey) (PDB code [[3jbw]])'>
The '''RAG (Recombination Activating Gene) complex protein''' or '''V(D)J recombination-activating protein''' is composed of two subunits, RAG-1 and RAG-2. RAG-1 and RAG-2 are critical in T and B cell maturation, promoting an adaptive immune response.  
The '''RAG (Recombination Activating Gene) complex protein''' or '''V(D)J recombination-activating protein''' is composed of two subunits, RAG-1 and RAG-2. RAG-1 and RAG-2 are critical in T and B cell maturation, promoting an adaptive immune response.  
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<scene name='77/778335/Rag2/1'> RAG2</scene> contains a plant homeodomain (PHD) near its C terminus (RAG2-PHD). This is unique because when a peptide is not being modified, a peptide N-terminal occupies the binding site, meaning that it is self-regulated. There is significantly less structural data on RAG2 due to a debate about the function of RAG2. Many challenge the belief that RAG2 cuts the RSS sequence, believing instead that RAG2 acts as a regulatory component to the complex.  
<scene name='77/778335/Rag2/1'> RAG2</scene> contains a plant homeodomain (PHD) near its C terminus (RAG2-PHD). This is unique because when a peptide is not being modified, a peptide N-terminal occupies the binding site, meaning that it is self-regulated. There is significantly less structural data on RAG2 due to a debate about the function of RAG2. Many challenge the belief that RAG2 cuts the RSS sequence, believing instead that RAG2 acts as a regulatory component to the complex.  
== 3D Structures of recombination-activating gene ==
[[Recombination-activating gene 3D structures]]


</StructureSection>
</StructureSection>
== 3D Structures of V(D)J recombination-activating protein ==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*RAG1
**[[3gna]], [[3gnb]] – mRAG1 nonamer binding domain 389-456 + DNA – mouse <br />
*RAG2
**[[2jwo]] – mRAG2 PHD finger 414-487 - NMR <br />
*RAG1+RAG2
**[[4wwx]] – mRAG1 391-1008 + RAG2  <br />
**[[5ze0]], [[5zdz]], [[5ze1]], [[5ze2]] – mRAG1 391-1008 + RAG2 (mutant) + high mobility group protein 1 + DNA<br />
**[[6cik]], [[6cil]], [[6cim]] – mRAG1 391-1008 + RAG2 + high mobility group protein 1 + DNA<br />
**[[3jbw]], [[3jbx]], [[3jby]] – mRAG1 271-1031 + RAG2 + DNA – Cryo EM<br />
**[[6cg0]], [[6cij]] – mRAG1 + RAG2 (mutant) + high mobility group protein 1 + DNA – Cryo EM<br />
**[[6dbi]], [[6dbl]], [[6dbo]], [[6dbq]], [[6dbj]], [[6dbr]], [[6dbt]], [[6dbu]], [[6dbw]], [[6dbx]], [[6dbv]] – RAG1 271-1031 + RAG2 + DNA – zebrafish -Cryo EM<br />
}}


== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]

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Leah Umbarger, Michal Harel, Jaime Prilusky
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