Sandbox Reserved 896: Difference between revisions

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==General Overview==

Human bromodomain-containing protein 2 (BRD2) is a highly conserved and ubiquitously expressed protein involved in transcriptional regulation and recognition of post-translational histone modifications. BRD2 is a bromodomain and extra-terminal domain (BET) family protein, which are characterized by the presence of two adjacent bromodomains as well as an extra-terminal domain. Bromodomain and extra terminal domain (BET) family proteins are a group of related proteins involved in the specific recognition of acetylated lysine residues on chromatin and subsequent transcriptional activation [2]. As a BET protein, BRD2 follows this structural motif with its structure consisting of ~~bromodomain 1 (BRD2-BD1)~~ at the C-terminus, bromodomain 2 (BRD2-BD2), and ~~an N~~-~~extra~~-~~terminal (NET) domain~~. Human BRD2 is encoded by the gene BRD2, which consists of 11 exons that cover more than 6 kb of genomic DNA [1]. This gene was formerly known as really interesting new gene 3 (RING3) but was later renamed to BRD2.

Human bromodomain-containing protein 2 (BRD2) is a highly conserved and ubiquitously expressed protein involved in transcriptional regulation and recognition of post-translational histone modifications. BRD2 is a bromodomain and extra-terminal domain (BET) family protein, which are characterized by the presence of two adjacent bromodomains as well as an extra-terminal domain. Bromodomain and extra terminal domain (BET) family proteins are a group of related proteins involved in the specific recognition of acetylated lysine residues on chromatin and subsequent transcriptional activation [2]. As a BET protein, BRD2 follows this structural motif with its structure consisting of an NET domain at the N-terminus, followed by bromodomain 2 (BRD2-BD2), and finally bromodomain 1 (BRD2-BD1) at the C-terminus. Human BRD2 is encoded by the gene BRD2, which consists of 11 exons that cover more than 6 kb of genomic DNA [1]. This gene was formerly known as really interesting new gene 3 (RING3) but was later renamed to BRD2.

[[Media:BRDTry4.mp4]]

== Function ==

Human BRD2 protein is a Serine-Threonine kinase and chromatin regulator found ubiquitously amongst the nuclear envelope of 223 tissue types. The activity of BRD2 is increased during cell proliferation. BRD2 specifically recognizes an N-acetyl-lysine residue at position 12 of histone H4 via a homo-2-mer complex of BD1 domains. This recognition is mediated through the binding of the hypoacetylated side chain of lysine at position 8 of H4 with the interface between dimerized BRD2-BD1 domains [3]. BRD2-BD1 and BD2 preferentially bind diacetylated peptides with optimal spacing between N-acetyl-lysine residues. BD1 has particular affinity for diacetylated lysine residues at position 5 and 8 of H4, whereas BD2 is significantly more promiscuous [6]. It is presumed that one of the functions of this recognition is to prevent deletion or erasure of post-translational histone markers during the mitotic cell cycle. The transcriptional regulation activity of BRD2 is also mediated through its positive regulation of E2F-dependent cell cycle progression (direct stimulation of E2F reporter activity) [1]. As E2F’s central function is to promote the synthesis of proteins needed for G1 to S transition, BRD2-BD1 is directly implicated in the regulation of the cell cycle. BRD2-BD1 also interacts with latency-associated nuclear antigen 1 (LANA-1), a protein involved in Kaposi’s sarcoma-associated herpesvirus [5]. BRD2-BD2 is known to facilitate recruitment of other BET proteins to induce gene expression in specific phases of the cell cycle [6].

Human BRD2 protein is a Serine-Threonine kinase and chromatin regulator found ubiquitously amongst the nuclear envelope of 223 tissue types. The activity of BRD2 is increased during cell proliferation. BRD2 specifically recognizes an N-acetyl-lysine residue at position 12 of histone H4 [3]. BRD2-BD1 and BD2 preferentially bind diacetylated peptides with optimal spacing between N-acetyl-lysine residues. BD1 has particular affinity for diacetylated lysine residues at position 5 and 8 of H4, whereas BD2 is significantly more promiscuous [6]. It is presumed that one of the functions of this recognition is to prevent deletion or erasure of post-translational histone markers during the mitotic cell cycle. The transcriptional regulation activity of BRD2 is also mediated through its positive regulation of E2F-dependent cell cycle progression (direct stimulation of E2F reporter activity) [1]. As E2F’s central function is to promote the synthesis of proteins needed for G1 to S transition, BRD2-BD1 is directly implicated in the regulation of the cell cycle. BRD2-BD1 also interacts with latency-associated nuclear antigen 1 (LANA-1), a protein involved in Kaposi’s sarcoma-associated herpesvirus [5]. BRD2-BD2 is known to facilitate recruitment of other BET proteins to induce gene expression in specific phases of the cell cycle [6].

[[Image:BRD2BD1SurfaceView.png]]

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 ==General Overview==
-Human bromodomain-containing protein 2 (BRD2) is a highly conserved and ubiquitously expressed protein involved in transcriptional regulation and recognition of post-translational histone modifications. BRD2 is a bromodomain and extra-terminal domain (BET) family protein, which are characterized by the presence of two adjacent bromodomains as well as an extra-terminal domain. Bromodomain and extra terminal domain (BET) family proteins are a group of related proteins involved in the specific recognition of acetylated lysine residues on chromatin and subsequent transcriptional activation [2]. As a BET protein, BRD2 follows this structural motif with its structure consisting of bromodomain 1 (BRD2-BD1) at the C-terminus, bromodomain 2 (BRD2-BD2), and an N-extra-terminal (NET) domain. Human BRD2 is encoded by the gene BRD2, which consists of 11 exons that cover more than 6 kb of genomic DNA [1]. This gene was formerly known as really interesting new gene 3 (RING3) but was later renamed to BRD2.
+Human bromodomain-containing protein 2 (BRD2) is a highly conserved and ubiquitously expressed protein involved in transcriptional regulation and recognition of post-translational histone modifications. BRD2 is a bromodomain and extra-terminal domain (BET) family protein, which are characterized by the presence of two adjacent bromodomains as well as an extra-terminal domain. Bromodomain and extra terminal domain (BET) family proteins are a group of related proteins involved in the specific recognition of acetylated lysine residues on chromatin and subsequent transcriptional activation [2]. As a BET protein, BRD2 follows this structural motif with its structure consisting of an NET domain at the N-terminus, followed by bromodomain 2 (BRD2-BD2), and finally bromodomain 1 (BRD2-BD1) at the C-terminus. Human BRD2 is encoded by the gene BRD2, which consists of 11 exons that cover more than 6 kb of genomic DNA [1]. This gene was formerly known as really interesting new gene 3 (RING3) but was later renamed to BRD2.
 [[Media:BRDTry4.mp4]]
 == Function ==
-Human BRD2 protein is a Serine-Threonine kinase and chromatin regulator found ubiquitously amongst the nuclear envelope of 223 tissue types. The activity of BRD2 is increased during cell proliferation. BRD2 specifically recognizes an N-acetyl-lysine residue at position 12 of histone H4 via a homo-2-mer complex of BD1 domains. This recognition is mediated through the binding of the hypoacetylated side chain of lysine at position 8 of H4 with the interface between dimerized BRD2-BD1 domains [3]. BRD2-BD1 and BD2 preferentially bind diacetylated peptides with optimal spacing between N-acetyl-lysine residues. BD1 has particular affinity for diacetylated lysine residues at position 5 and 8 of H4, whereas BD2 is significantly more promiscuous [6]. It is presumed that one of the functions of this recognition is to prevent deletion or erasure of post-translational histone markers during the mitotic cell cycle. The transcriptional regulation activity of BRD2 is also mediated through its positive regulation of E2F-dependent cell cycle progression (direct stimulation of E2F reporter activity) [1]. As E2F’s central function is to promote the synthesis of proteins needed for G1 to S transition, BRD2-BD1 is directly implicated in the regulation of the cell cycle. BRD2-BD1 also interacts with latency-associated nuclear antigen 1 (LANA-1), a protein involved in Kaposi’s sarcoma-associated herpesvirus [5]. BRD2-BD2 is known to facilitate recruitment of other BET proteins to induce gene expression in specific phases of the cell cycle [6].
+Human BRD2 protein is a Serine-Threonine kinase and chromatin regulator found ubiquitously amongst the nuclear envelope of 223 tissue types. The activity of BRD2 is increased during cell proliferation. BRD2 specifically recognizes an N-acetyl-lysine residue at position 12 of histone H4 [3]. BRD2-BD1 and BD2 preferentially bind diacetylated peptides with optimal spacing between N-acetyl-lysine residues. BD1 has particular affinity for diacetylated lysine residues at position 5 and 8 of H4, whereas BD2 is significantly more promiscuous [6]. It is presumed that one of the functions of this recognition is to prevent deletion or erasure of post-translational histone markers during the mitotic cell cycle. The transcriptional regulation activity of BRD2 is also mediated through its positive regulation of E2F-dependent cell cycle progression (direct stimulation of E2F reporter activity) [1]. As E2F’s central function is to promote the synthesis of proteins needed for G1 to S transition, BRD2-BD1 is directly implicated in the regulation of the cell cycle. BRD2-BD1 also interacts with latency-associated nuclear antigen 1 (LANA-1), a protein involved in Kaposi’s sarcoma-associated herpesvirus [5]. BRD2-BD2 is known to facilitate recruitment of other BET proteins to induce gene expression in specific phases of the cell cycle [6].
 [[Image:BRD2BD1SurfaceView.png]]