Sandbox Reserved 1455: Difference between revisions
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<scene name='77/778335/Rag-1_dimer_and_dna/1'>This</scene> is the asymmetrical crystal structure of RAG1, featuring the dimer bound to a DNA molecule. In reality, the dimer binds two DNA molecules, one bound in a cis configuration and the other bound in trans configuration. | <scene name='77/778335/Rag-1_dimer_and_dna/1'>This</scene> is the asymmetrical crystal structure of RAG1, featuring the dimer bound to a DNA molecule. In reality, the dimer binds two DNA molecules, one bound in a cis configuration and the other bound in trans configuration. | ||
<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. | <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. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
