Recombination-activating gene: Difference between revisions
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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> | ||
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**[[3gna]], [[3gnb]] – mRAG1 nonamer binding domain 389-456 + DNA – mouse <br /> | **[[3gna]], [[3gnb]] – mRAG1 nonamer binding domain 389-456 + DNA – mouse <br /> | ||
**[[1rmd]] – mRAG1 dimerization domain 265-380 <br /> | |||
*RAG2 | *RAG2 | ||
**[[2jwo]] – mRAG2 PHD finger 414-487 - NMR <br /> | **[[2jwo]] – mRAG2 PHD finger 414-487 - NMR <br /> | ||
**[[2v83]], [[2v85]], [[2v86]], [[2v87]], [[2v88]], [[2v89]] – mRAG2 PHD finger + histone peptide <br /> | |||
*RAG1+RAG2 | *RAG1+RAG2 | ||
