Proteopedia - User contributions [en]

Recombination-activating gene

2018-04-30T20:12:27Z

Leah Umbarger: New page: ==Recombination Activating Gene Complex== <StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''> The RAG complex protein is composed of tw...

==Recombination Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''>
The RAG complex 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.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. Gene recombination, known as Variable, Diverse, and Joining (V(D)J) recombination, is only found in developing B and T cells. V(D)J recombination results in unique amino acid sequences. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. Within the human body, the developing antibodies, each composed of heavy and light chains. Within the heavy chain, DJ recombination occurs first, and then V and DJ recombination occurs. The light chain, however, only has VJ recombination. The newly formed interactions between each gene segment gives rise to a unique heavy and unique light chain. The interaction between heavy and light chains form the classic antibody structure, promoting the function. The process of V(D)J recombination cannot occur without the help of the RAG complex <ref name= "Article 1" >Jones, Pat, et al. Immunology. 7th ed., W.H. Freeman and Company, 2013. </ref>.

RAG-1 and RAG-2 appear in the body as one complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain <ref name= "Article2" >Sadofsky, Moshe J. “The RAG Proteins in V(D)J Recombination: More than Just a Nuclease.” Nucleic Acids Research 29.7 (2001): 1399–1409. Print. </ref>. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends <ref name= "Article1" >Akamatsu, Yoshiko, and Marjorie A. Oettinger. “Distinct Roles of RAG1 and RAG2 in Binding the V(D)J Recombination Signal Sequences.” Molecular and Cellular Biology 18.8 (1998): 4670–4678. Print.</ref>.

== Disease ==
Mutated RAG-1 or RAG-2 prevents a fully functional immune system from developing. Defects in RAG1 or RAG2 cause impaired V(D)J recombination and this leads to defective expression of the pre-TCR and pre-BCR, a critical event in the development of T cells and B cells.
In classical experiments, null mutations of the RAG 1 and RAG 2 allele cause severe immunodeficiency disease (SCID), wherein B and T cell development does not occur.
In vivo experiments with RAG1 or RAG2 deficiency reveal that the complex can be partially mutated. In this case, the semi-functional RAG complex is linked to Omenn Syndrome. Omenn Syndrome is associated with severe immunodeficiency <ref>DOI: 10.1056/NEJMoa073966</ref>.

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments <ref name= "Article 5" >Levy, Daniel, director. VDJ Gene Recombination. VDJ Gene Recombination , 10 Apr. 2014, www.youtube.com/watch?v=QTOBSFJWogE. </ref>. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens <ref name= "Article 3" >“RAG1 Gene - Genetics Home Reference.” U.S. National Library of Medicine, National Institutes of Health, ghr.nlm.nih.gov/gene/RAG1. </ref>

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex.

<scene name='77/778335/Rag-1/1'>This</scene> is the dimerization formation of RAG-1. It features four zinc binding-motifs that assist in RAG1 binding to the specific recombination signal sequence.
<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. 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>
== References ==
<references/>

Sandbox Reserved 1455

2018-04-30T20:04:18Z

Leah Umbarger:

{{Sandbox_Reserved_Telford2018}}
==Recombination Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''>
The RAG complex 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.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. Gene recombination, known as Variable, Diverse, and Joining (V(D)J) recombination, is only found in developing B and T cells. V(D)J recombination results in unique amino acid sequences. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. Within the human body, the developing antibodies, each composed of heavy and light chains. Within the heavy chain, DJ recombination occurs first, and then V and DJ recombination occurs. The light chain, however, only has VJ recombination. The newly formed interactions between each gene segment gives rise to a unique heavy and unique light chain. The interaction between heavy and light chains form the classic antibody structure, promoting the function. The process of V(D)J recombination cannot occur without the help of the RAG complex <ref name= "Article 1" >Jones, Pat, et al. Immunology. 7th ed., W.H. Freeman and Company, 2013. </ref>.

RAG-1 and RAG-2 appear in the body as one complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain <ref name= "Article2" >Sadofsky, Moshe J. “The RAG Proteins in V(D)J Recombination: More than Just a Nuclease.” Nucleic Acids Research 29.7 (2001): 1399–1409. Print. </ref>. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends <ref name= "Article1" >Akamatsu, Yoshiko, and Marjorie A. Oettinger. “Distinct Roles of RAG1 and RAG2 in Binding the V(D)J Recombination Signal Sequences.” Molecular and Cellular Biology 18.8 (1998): 4670–4678. Print.</ref>.

== Disease ==
Mutated RAG-1 or RAG-2 prevents a fully functional immune system from developing. Defects in RAG1 or RAG2 cause impaired V(D)J recombination and this leads to defective expression of the pre-TCR and pre-BCR, a critical event in the development of T cells and B cells.
In classical experiments, null mutations of the RAG 1 and RAG 2 allele cause severe immunodeficiency disease (SCID), wherein B and T cell development does not occur.
In vivo experiments with RAG1 or RAG2 deficiency reveal that the complex can be partially mutated. In this case, the semi-functional RAG complex is linked to Omenn Syndrome. Omenn Syndrome is associated with severe immunodeficiency <ref>DOI: 10.1056/NEJMoa073966</ref>.

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments <ref name= "Article 5" >Levy, Daniel, director. VDJ Gene Recombination. VDJ Gene Recombination , 10 Apr. 2014, www.youtube.com/watch?v=QTOBSFJWogE. </ref>. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens <ref name= "Article 3" >“RAG1 Gene - Genetics Home Reference.” U.S. National Library of Medicine, National Institutes of Health, ghr.nlm.nih.gov/gene/RAG1. </ref>

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex.

<scene name='77/778335/Rag-1/1'>This</scene> is the dimerization formation of RAG-1. It features four zinc binding-motifs that assist in RAG1 binding to the specific recombination signal sequence.
<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. 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>
== References ==
<references/>

Sandbox Reserved 1455

2018-04-30T19:52:26Z

Leah Umbarger:

{{Sandbox_Reserved_Telford2018}}
==Recombination Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''>
The RAG complex 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.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. Gene recombination, known as V(D)J recombination, is only found in developing B and T cells. V(D)J recombination results in unique amino acid sequences. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. Within the human body, the developing antibodies, each composed of heavy and light chains. Within the heavy chain, DJ recombination occurs first, and then V and DJ recombination occurs. The light chain, however, only has VJ recombination. The newly formed interactions between each gene segment gives rise to a unique heavy and unique light chain. The interaction between heavy and light chains form the classic antibody structure, promoting the function. The process of V(D)J recombination cannot occur without the help of the RAG complex <ref name= "Article 1" >Jones, Pat, et al. Immunology. 7th ed., W.H. Freeman and Company, 2013. </ref>.

RAG-1 and RAG-2 appear in the body as one complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain <ref name= "Article2" >Sadofsky, Moshe J. “The RAG Proteins in V(D)J Recombination: More than Just a Nuclease.” Nucleic Acids Research 29.7 (2001): 1399–1409. Print. </ref>. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends <ref name= "Article1" >Akamatsu, Yoshiko, and Marjorie A. Oettinger. “Distinct Roles of RAG1 and RAG2 in Binding the V(D)J Recombination Signal Sequences.” Molecular and Cellular Biology 18.8 (1998): 4670–4678. Print.</ref>.

== Disease ==
Mutated RAG-1 or RAG-2 prevents a fully functional immune system from developing. Defects in RAG1 or RAG2 cause impaired V(D)J recombination and this leads to defective expression of the pre-TCR and pre-BCR, a critical event in the development of T cells and B cells.
In classical experiments, null mutations of the RAG 1 and RAG 2 allele cause severe immunodeficiency disease (SCID), wherein B and T cell development does not occur.
In vivo experiments with RAG1 or RAG2 deficiency reveal that the complex can be partially mutated. In this case, the semi-functional RAG complex is linked to Omenn Syndrome. Omenn Syndrome is associated with severe immunodeficiency <ref>DOI: 10.1056/NEJMoa073966</ref>.

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments <ref name= "Article 5" >Levy, Daniel, director. VDJ Gene Recombination. VDJ Gene Recombination , 10 Apr. 2014, www.youtube.com/watch?v=QTOBSFJWogE. </ref>. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens <ref name= "Article 3" >“RAG1 Gene - Genetics Home Reference.” U.S. National Library of Medicine, National Institutes of Health, ghr.nlm.nih.gov/gene/RAG1. </ref>

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex.

<scene name='77/778335/Rag-1/1'>This</scene> is the dimerization formation of RAG-1. It features four zinc binding-motifs that assist in RAG1 binding to the specific recombination signal sequence.
<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. 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>
== References ==
<references/>

Sandbox Reserved 1455

2018-04-30T19:51:19Z

Leah Umbarger:

{{Sandbox_Reserved_Telford2018}}
==Recombination Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''>
The RAG complex 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.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. Gene recombination, known as V(D)J recombination, is only found in developing B and T cells. V(D)J recombination results in unique amino acid sequences. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. Within the human body, the developing antibodies, each composed of heavy and light chains. Within the heavy chain, DJ recombination occurs first, and then V and DJ recombination occurs. The light chain, however, only has VJ recombination. The newly formed interactions between each gene segment gives rise to a unique heavy and unique light chain. The interaction between heavy and light chains form the classic antibody structure, promoting the function. The process of V(D)J recombination cannot occur without the help of the RAG complex <ref name= "Article 1" >Jones, Pat, et al. Immunology. 7th ed., W.H. Freeman and Company, 2013. </ref>.

RAG-1 and RAG-2 appear in the body as one complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain <ref name= "Article2" >Sadofsky, Moshe J. “The RAG Proteins in V(D)J Recombination: More than Just a Nuclease.” Nucleic Acids Research 29.7 (2001): 1399–1409. Print. </ref>. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends <ref name= "Article1" >Akamatsu, Yoshiko, and Marjorie A. Oettinger. “Distinct Roles of RAG1 and RAG2 in Binding the V(D)J Recombination Signal Sequences.” Molecular and Cellular Biology 18.8 (1998): 4670–4678. Print.</ref>.

== Disease ==
Mutated RAG-1 or RAG-2 prevents a fully functional immune system from developing. Defects in RAG1 or RAG2 cause impaired V(D)J recombination and this leads to defective expression of the pre-TCR and pre-BCR, a critical event in the development of T cells and B cells.
In classical experiments, null mutations of the RAG 1 and RAG 2 allele cause severe immunodeficiency disease (SCID), wherein B and T cell development does not occur.
In vivo experiments with RAG1 or RAG2 deficiency reveal that the complex can be partially mutated. In this case, the semi-functional RAG complex is linked to Omenn Syndrome. Omenn Syndrome is associated with severe immunodeficiency <ref>DOI: 10.1111/j.1399-0004.2004.00227</ref>.

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments <ref name= "Article 5" >Levy, Daniel, director. VDJ Gene Recombination. VDJ Gene Recombination , 10 Apr. 2014, www.youtube.com/watch?v=QTOBSFJWogE. </ref>. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens <ref name= "Article 3" >“RAG1 Gene - Genetics Home Reference.” U.S. National Library of Medicine, National Institutes of Health, ghr.nlm.nih.gov/gene/RAG1. </ref>

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex.

<scene name='77/778335/Rag-1/1'>This</scene> is the dimerization formation of RAG-1. It features four zinc binding-motifs that assist in RAG1 binding to the specific recombination signal sequence.
<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. 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>
== References ==
<references/>

Sandbox Reserved 1455

2018-04-30T19:50:33Z

Leah Umbarger:

{{Sandbox_Reserved_Telford2018}}
==Recombination Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''>
The RAG complex 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.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. Gene recombination, known as V(D)J recombination, is only found in developing B and T cells. V(D)J recombination results in unique amino acid sequences. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. Within the human body, the developing antibodies, each composed of heavy and light chains. Within the heavy chain, DJ recombination occurs first, and then V and DJ recombination occurs. The light chain, however, only has VJ recombination. The newly formed interactions between each gene segment gives rise to a unique heavy and unique light chain. The interaction between heavy and light chains form the classic antibody structure, promoting the function. The process of V(D)J recombination cannot occur without the help of the RAG complex <ref name= "Article 1" >Jones, Pat, et al. Immunology. 7th ed., W.H. Freeman and Company, 2013. </ref>.

RAG-1 and RAG-2 appear in the body as one complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain <ref name= "Article2" >Sadofsky, Moshe J. “The RAG Proteins in V(D)J Recombination: More than Just a Nuclease.” Nucleic Acids Research 29.7 (2001): 1399–1409. Print. </ref>. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends <ref name= "Article1" >Akamatsu, Yoshiko, and Marjorie A. Oettinger. “Distinct Roles of RAG1 and RAG2 in Binding the V(D)J Recombination Signal Sequences.” Molecular and Cellular Biology 18.8 (1998): 4670–4678. Print.</ref>.

== Disease ==
Mutated RAG-1 or RAG-2 prevents a fully functional immune system from developing. Defects in RAG1 or RAG2 cause impaired V(D)J recombination and this leads to defective expression of the pre-TCR and pre-BCR, a critical event in the development of T cells and B cells.
In classical experiments, null mutations of the RAG 1 and RAG 2 allele cause severe immunodeficiency disease (SCID), wherein B and T cell development does not occur.
In vivo experiments with RAG1 or RAG2 deficiency reveal that the complex can be partially mutated. In this case, the semi-functional RAG complex is linked to Omenn Syndrome. Omenn Syndrome is associated with severe immunodeficiency <ref>DOI: 10.1111/j.1399-0004.2004.00227.x.</ref>.

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments <ref name= "Article 5" >Levy, Daniel, director. VDJ Gene Recombination. VDJ Gene Recombination , 10 Apr. 2014, www.youtube.com/watch?v=QTOBSFJWogE. </ref>. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens <ref name= "Article 3" >“RAG1 Gene - Genetics Home Reference.” U.S. National Library of Medicine, National Institutes of Health, ghr.nlm.nih.gov/gene/RAG1. </ref>

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex.

<scene name='77/778335/Rag-1/1'>This</scene> is the dimerization formation of RAG-1. It features four zinc binding-motifs that assist in RAG1 binding to the specific recombination signal sequence.
<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. 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>
== References ==
<references/>

Sandbox Reserved 1455

2018-04-30T19:48:25Z

Leah Umbarger:

{{Sandbox_Reserved_Telford2018}}
==Recombination Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''>
The RAG complex 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.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. Gene recombination, known as V(D)J recombination, is only found in developing B and T cells. V(D)J recombination results in unique amino acid sequences. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. Within the human body, the developing antibodies, each composed of heavy and light chains. Within the heavy chain, DJ recombination occurs first, and then V and DJ recombination occurs. The light chain, however, only has VJ recombination. The newly formed interactions between each gene segment gives rise to a unique heavy and unique light chain. The interaction between heavy and light chains form the classic antibody structure, promoting the function. The process of V(D)J recombination cannot occur without the help of the RAG complex <ref name= "Article 1" >Jones, Pat, et al. Immunology. 7th ed., W.H. Freeman and Company, 2013. </ref>.

RAG-1 and RAG-2 appear in the body as one complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain <ref name= "Article2" >Sadofsky, Moshe J. “The RAG Proteins in V(D)J Recombination: More than Just a Nuclease.” Nucleic Acids Research 29.7 (2001): 1399–1409. Print. </ref>. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends <ref name= "Article1" >Akamatsu, Yoshiko, and Marjorie A. Oettinger. “Distinct Roles of RAG1 and RAG2 in Binding the V(D)J Recombination Signal Sequences.” Molecular and Cellular Biology 18.8 (1998): 4670–4678. Print.</ref>.

== Disease ==
Mutated RAG-1 or RAG-2 prevents a fully functional immune system from developing. Defects in RAG1 or RAG2 cause impaired V(D)J recombination and this leads to defective expression of the pre-TCR and pre-BCR, a critical event in the development of T cells and B cells.
In classical experiments, null mutations of the RAG 1 and RAG 2 allele cause severe immunodeficiency disease (SCID), wherein B and T cell development does not occur.
In vivo experiments with RAG1 or RAG2 deficiency reveal that the complex can be partially mutated. In this case, the semi-functional RAG complex is linked to Omenn Syndrome. Omenn Syndrome is associated with severe immunodeficiency <ref name= "Article 4" >Tabori, U, et al. “Detection of RAG Mutations and Prenatal Diagnosis in Families Presenting with Either T-B- Severe Combined Immunodeficiency or Omenn's Syndrome.” Clinical Genetics, vol. 65, no. 4, 2004, pp. 322–326., doi:10.1111/j.1399-0004.2004.00227.x. </ref>.

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments <ref name= "Article 5" >Levy, Daniel, director. VDJ Gene Recombination. VDJ Gene Recombination , 10 Apr. 2014, www.youtube.com/watch?v=QTOBSFJWogE. </ref>. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens <ref name= "Article 3" >“RAG1 Gene - Genetics Home Reference.” U.S. National Library of Medicine, National Institutes of Health, ghr.nlm.nih.gov/gene/RAG1. </ref>

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex.

<scene name='77/778335/Rag-1/1'>This</scene> is the dimerization formation of RAG-1. It features four zinc binding-motifs that assist in RAG1 binding to the specific recombination signal sequence.
<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. 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>
== References ==
<references/>

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==Recombination Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''>
The RAG complex 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.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. Gene recombination, known as V(D)J recombination, is only found in developing B and T cells. V(D)J recombination results in unique amino acid sequences. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. Within the human body, the developing antibodies, each composed of heavy and light chains. Within the heavy chain, DJ recombination occurs first, and then V and DJ recombination occurs. The light chain, however, only has VJ recombination. The newly formed interactions between each gene segment gives rise to a unique heavy and unique light chain. The interaction between heavy and light chains form the classic antibody structure, promoting the function. The process of V(D)J recombination cannot occur without the help of the RAG complex >ref name= "Article 1" >Jones, Pat, et al. Immunology. 7th ed., W.H. Freeman and Company, 2013. </ref>.

RAG-1 and RAG-2 appear in the body as one complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain <ref name= "Article2" >Sadofsky, Moshe J. “The RAG Proteins in V(D)J Recombination: More than Just a Nuclease.” Nucleic Acids Research 29.7 (2001): 1399–1409. Print. </ref>. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends <ref name= "Article1" >Akamatsu, Yoshiko, and Marjorie A. Oettinger. “Distinct Roles of RAG1 and RAG2 in Binding the V(D)J Recombination Signal Sequences.” Molecular and Cellular Biology 18.8 (1998): 4670–4678. Print.</ref>.

== Disease ==
Mutated RAG-1 or RAG-2 prevents a fully functional immune system from developing. Defects in RAG1 or RAG2 cause impaired V(D)J recombination and this leads to defective expression of the pre-TCR and pre-BCR, a critical event in the development of T cells and B cells.
In classical experiments, null mutations of the RAG 1 and RAG 2 allele cause severe immunodeficiency disease (SCID), wherein B and T cell development does not occur.
In vivo experiments with RAG1 or RAG2 deficiency reveal that the complex can be partially mutated. In this case, the semi-functional RAG complex is linked to Omenn Syndrome. Omenn Syndrome is associated with severe immunodeficiency <ref name= "Article 4" >Tabori, U, et al. “Detection of RAG Mutations and Prenatal Diagnosis in Families Presenting with Either T-B- Severe Combined Immunodeficiency or Omenn's Syndrome.” Clinical Genetics, vol. 65, no. 4, 2004, pp. 322–326., doi:10.1111/j.1399-0004.2004.00227.x. </ref>.

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments <ref name= "Article 5" >Levy, Daniel, director. VDJ Gene Recombination. VDJ Gene Recombination , 10 Apr. 2014, www.youtube.com/watch?v=QTOBSFJWogE. </ref>. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens <ref name= "Article 3" >“RAG1 Gene - Genetics Home Reference.” U.S. National Library of Medicine, National Institutes of Health, ghr.nlm.nih.gov/gene/RAG1. </ref>

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex.

<scene name='77/778335/Rag-1/1'>This</scene> is the dimerization formation of RAG-1. It features four zinc binding-motifs that assist in RAG1 binding to the specific recombination signal sequence.
<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. 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>
== References ==
<references/>

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{{Sandbox_Reserved_Telford2018}}
==Recombination Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''>
The RAG complex 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.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. RAG-1 and RAG-2 appear in the body as a complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain <ref name= "Article2" >Sadofsky, Moshe J. “The RAG Proteins in V(D)J Recombination: More than Just a Nuclease.” Nucleic Acids Research 29.7 (2001): 1399–1409. Print. </ref>. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends <ref name= "Article1" >Akamatsu, Yoshiko, and Marjorie A. Oettinger. “Distinct Roles of RAG1 and RAG2 in Binding the V(D)J Recombination Signal Sequences.” Molecular and Cellular Biology 18.8 (1998): 4670–4678. Print.</ref>.

== Disease ==
Mutated RAG-1 or RAG-2 prevents a fully functional immune system from developing. Defects in RAG1 or RAG2 cause impaired V(D)J recombination and this leads to defective expression of the pre-TCR and pre-BCR, a critical event in the development of T cells and B cells.
In classical experiments, null mutations of the RAG 1 and RAG 2 allele cause severe immunodeficiency disease (SCID), wherein B and T cell development does not occur.
In vivo experiments with RAG1 or RAG2 deficiency reveal that the complex can be partially mutated. In this case, the semi-functional RAG complex is linked to Omenn Syndrome. Omenn Syndrome is associated with severe immunodeficiency <ref name= "Article 4" >Tabori, U, et al. “Detection of RAG Mutations and Prenatal Diagnosis in Families Presenting with Either T-B- Severe Combined Immunodeficiency or Omenn's Syndrome.” Clinical Genetics, vol. 65, no. 4, 2004, pp. 322–326., doi:10.1111/j.1399-0004.2004.00227.x. </ref>.

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments <ref name= "Article 5" >Levy, Daniel, director. VDJ Gene Recombination. VDJ Gene Recombination , 10 Apr. 2014, www.youtube.com/watch?v=QTOBSFJWogE. </ref>. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens <ref name= "Article 3" >“RAG1 Gene - Genetics Home Reference.” U.S. National Library of Medicine, National Institutes of Health, ghr.nlm.nih.gov/gene/RAG1. </ref>

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex.

<scene name='77/778335/Rag-1/1'>This</scene> is the dimerization formation of RAG-1. It features four zinc binding-motifs that assist in RAG1 binding to the specific recombination signal sequence.
<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. 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>
== References ==
<references/>

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Leah Umbarger:

{{Sandbox_Reserved_Telford2018}}
==Recombination Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''>
The RAG complex 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.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. RAG-1 and RAG-2 appear in the body as a complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain <ref name= "Article2" >Sadofsky, Moshe J. “The RAG Proteins in V(D)J Recombination: More than Just a Nuclease.” Nucleic Acids Research 29.7 (2001): 1399–1409. Print. </ref>. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends <ref name= "Article1" >Akamatsu, Yoshiko, and Marjorie A. Oettinger. “Distinct Roles of RAG1 and RAG2 in Binding the V(D)J Recombination Signal Sequences.” Molecular and Cellular Biology 18.8 (1998): 4670–4678. Print.</ref>.

== Disease ==
Mutated RAG-1 or RAG-2 prevents a fully functional immune system from developing. Defects in RAG1 or RAG2 cause impaired V(D)J recombination and this leads to defective expression of the pre-TCR and pre-BCR, a critical event in the development of T cells and B cells.
In classical experiments, null mutations of the RAG 1 and RAG 2 allele cause severe immunodeficiency disease (SCID), wherein B and T cell development does not occur.
In vivo experiments with RAG1 or RAG2 deficiency reveal that the complex can be partially mutated. In this case, the semi-functional RAG complex is linked to Omenn Syndrome. Omenn Syndrome is associated with severe immunodeficiency.

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex.

<scene name='77/778335/Rag-1/1'>This</scene> is the dimerization formation of RAG-1. It features four zinc binding-motifs that assist in RAG1 binding to the specific recombination signal sequence.
<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. 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>
== References ==
<references/>

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==Recombination Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''>
The RAG complex 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.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. RAG-1 and RAG-2 appear in the body as a complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends <ref name= "Article1" >Akamatsu, Yoshiko, and Marjorie A. Oettinger. “Distinct Roles of RAG1 and RAG2 in Binding the V(D)J Recombination Signal Sequences.” Molecular and Cellular Biology 18.8 (1998): 4670–4678. Print.</ref>.

== Disease ==
Mutated RAG-1 or RAG-2 prevents a fully functional immune system from developing. Defects in RAG1 or RAG2 cause impaired V(D)J recombination and this leads to defective expression of the pre-TCR and pre-BCR, a critical event in the development of T cells and B cells.
In classical experiments, null mutations of the RAG 1 and RAG 2 allele cause severe immunodeficiency disease (SCID), wherein B and T cell development does not occur.
In vivo experiments with RAG1 or RAG2 deficiency reveal that the complex can be partially mutated. In this case, the semi-functional RAG complex is linked to Omenn Syndrome. Omenn Syndrome is associated with severe immunodeficiency.

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex.

<scene name='77/778335/Rag-1/1'>This</scene> is the dimerization formation of RAG-1. It features four zinc binding-motifs that assist in RAG1 binding to the specific recombination signal sequence.
<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. 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>
== References ==
<references/>

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==Recombination Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''>
The RAG complex 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.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. RAG-1 and RAG-2 appear in the body as a complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends <ref name= "Article1" >Akamatsu, Yoshiko, and Marjorie A. Oettinger. “Distinct Roles of RAG1 and RAG2 in Binding the V(D)J Recombination Signal Sequences.” Molecular and Cellular Biology 18.8 (1998): 4670–4678. Print.</ref>.

== Disease ==
Mutated RAG-1 or RAG-2 prevents a fully functional immune system from developing. Defects in RAG1 or RAG2 cause impaired V(D)J recombination and this leads to defective expression of the pre-TCR and pre-BCR, a critical event in the development of T cells and B cells.
In classical experiments, null mutations of the RAG 1 and RAG 2 allele cause severe immunodeficiency disease (SCID), wherein B and T cell development does not occur.
In vivo experiments with RAG1 or RAG2 deficiency reveal that the complex can be partially mutated. In this case, the semi-functional RAG complex is linked to Omenn Syndrome. Omenn Syndrome is associated with severe immunodeficiency.

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex.

<scene name='77/778335/Rag-1/1'>This</scene> is the dimerization formation of RAG-1. It features four zinc binding-motifs that assist in RAG1 binding to the specific recombination signal sequence.
<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. 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>
== References ==
<references/>

Akamatsu, Yoshiko, and Marjorie A. Oettinger. “Distinct Roles of RAG1 and RAG2 in Binding the V(D)J Recombination Signal Sequences.” Molecular and Cellular Biology 18.8 (1998): 4670–4678. Print.

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{{Sandbox_Reserved_Telford2018}}
==Recombination Activating Gene Complex==
<StructureSection load='3jbw' size='340' side='right' caption='Recombination Activating Gene Complex=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. RAG-1 and RAG-2 appear in the body as a complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends.

== Disease ==

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

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{{Sandbox_Reserved_Telford2018}}
==Recombination Activating Gene Complex==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. RAG-1 and RAG-2 appear in the body as a complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends.

== Disease ==

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

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{{Sandbox_Reserved_Telford2018}}
==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
This RAG complex protein allows the human body to have diverse immune response. Using both RAG-1 and RAG-2 together allows for recombination to occur to create cell receptors on both B and T cells. It is critical that the cell receptors are diverse in order to recognize a wide variety of pathogens and protect the body. RAG-1 and RAG-2 appear in the body as a complex. Both RAG-1 and RAG-2 are necessary for the function of the protein. RAG-1 cannot perform all of the functions by itself associated with the RAG protein; similarly, RAG-2 cannot perform all of the functions alone. The RAG-1 protein will bind to a specific recombination signal sequence within the V-J region of the light chain and the D-J segment along with the V-DJ segment of a heavy chain. Next, RAG-1 will bring the various segments within close proximity, looping the DNA between the segments out. RAG-2 will then cut the RSS sequence and a different protein will bind the two DNA ends.

== Disease ==

== Relevance ==
This protein is predominantly important during the B and T cell development. Because humans need to be well-protected from antigens, B cells and T cells must have a variety of proteins on their surface in order to recognize a variety of invaders. Causing these proteins to become diverse involves a series of segments known as Variable (V), Diversity (D), and Joining (J) segments. These segments can be arranged in many combinations of sequences that ensure variable surface proteins. Without the RAG protein, B and T cells would lack the ability to identify and destroy foreign pathogens

== Structural highlights ==
<scene name='77/778335/Rag_1/1'>Nucleic Acids</scene> found in RAG complex
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

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