Sandbox GGC5
From Proteopedia
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- | ==Structure of RAG1/2-DNA Strand Transfer Complex (paired conformation)== | ||
- | <StructureSection load='6XNY' size='340' side='right' caption='Structure of RAG1/2-DNA Strand Transfer Complex (Paired Conformation)' scene='75/752271/Rag_complex_background/1'> | ||
- | RAG1 is the catalytic component of the RAG Complex. Together with RAG2, the RAG Complex functions to create antibodies for virtually any antigen. | ||
- | == Function == | ||
- | RAG1 and RAG2 form the RAG Complex (RAG Recombinases), which is responsible for regulating the DNA cleavage phase during recombination. V(D)J recombination functions to produce a plethora of immune molecules in developing B and T-lymphocytes. The V stands for variable, D, diversity and J joining. RAG1 functions as the catalytic portion while RAG2, although not catalytic, is required for RAG1 to function. RAG1 creates a double-stranded break between the recombination signal sequences (RSS) and the adjacent coding sequence. This process is executed in the following way: introduction of a nick, creating a 3'-hydroxyl group which attacks the phosphodiester bond on the opposite strand. This is a direct transesterification reaction which results in four DNA ends. Histones also assist in the nicking and hairpinning of the strands. The result is the recombination of variable genes joining. Additionally to the role played in V(D)J, RAG also assists in pre-B cell allelic exclusion. This means that there is a recombination of the second allele. RAG1 also possess ubiquitin properties. | ||
== Disease == | == Disease == | ||
Revision as of 02:32, 26 April 2021
Contents |
Beta Lactamase: Class A
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
Function
Disease
Relevance
Structural highlights
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</StructureSection>