Sandbox Z-DNA: Difference between revisions
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=== Vaccinia virus E3L protein === | === Vaccinia virus E3L protein === | ||
E3L protein of vaccinia virus acts as an immune modulator and is required for replication of the virus. The <scene name='Sandbox_Z-DNA/E3lzalpha/2'> N-terminal</scene> region of E3L is similar to the Z-alpha domain of ADAR1 but has a lower binding affinity to Z-DNA than ADAR1 or DLM-1. Though the C-terminal of E3L is sufficient for viral replication it is the N-terminal which is responsible for pathogenicity. Mutations or deletions in the N-terminal region reduces the pathogenicity of the virus. Replacement of this domain with its corresponding analogues from ADAR1 or DLM-1 generates a chimeric virus which is as lethal as the wild type virus. Thus a drug which can block the binding of E3L to Z-DNA may be an effective therapy in preventing pathogenicity. Similarity of E3L to variola also suggests that such drugs might be effective against small pox. <ref name ='Wang'>PMID:17485386</ref><ref>PMID: 14757814</ref> ` | E3L protein of vaccinia virus acts as an immune modulator and is required for replication of the virus. The <scene name='Sandbox_Z-DNA/E3lzalpha/2'> N-terminal</scene> region of E3L is similar to the Z-alpha domain of ADAR1 but has a lower binding affinity to Z-DNA than ADAR1 or DLM-1. Though the C-terminal of E3L is sufficient for viral replication it is the N-terminal which is responsible for pathogenicity. Mutations or deletions in the N-terminal region reduces the pathogenicity of the virus. Replacement of this domain with its corresponding analogues from ADAR1 or DLM-1 generates a chimeric virus which is as lethal as the wild type virus. Thus a drug which can block the binding of E3L to Z-DNA may be an effective therapy in preventing pathogenicity. Similarity of E3L to variola also suggests that such drugs might be effective against small pox. <ref name ='Wang'>PMID:17485386</ref><ref name = 'E3L'>PMID: 14757814</ref> ` | ||
=== DLM-1 === | === DLM-1 === | ||
DLM-1 is also known as Z-DNA binding protein 1 (ZBP1). DLM-1 is a tumor associated gene expressed in lymphatic tissues and is upregulated in the peritoneal lining of mice with mouse ovarian ascites tumor. DLM-1 has two Z-DNA binding domains analogous to the Z-alpha and Z- beta domains in ADAR1. Comparison of Z-DNA binding of DLM-1 and ADAR1 revealed a common structure recognition core within the binding domain. However the role of DLM-1 binding to Z-DNA in tumor development is not known. | DLM-1 is also known as Z-DNA binding protein 1 (ZBP1). DLM-1 is a tumor associated gene expressed in lymphatic tissues and is upregulated in the peritoneal lining of mice with mouse ovarian ascites tumor. DLM-1 has two Z-DNA binding domains analogous to the Z-alpha and Z- beta domains in ADAR1. Comparison of Z-DNA binding of DLM-1 and ADAR1 revealed a common structure recognition core within the binding domain. However the role of DLM-1 binding to Z-DNA in tumor development is not known. | ||
Z-DNA binding proteins have common structural characteristics. Z-DNA binding domains of these proteins can substitute one another and thus can act as competitive inhibitors against one another. As explained above disruption in the Z-DNA binding region of E3L reduces its pathogenicity. All these observations are important pointers towards the biological importance of Z-DNA. | Z-DNA binding proteins have common structural characteristics. Z-DNA binding domains of these proteins can substitute one another and thus can act as competitive inhibitors against one another. As explained above disruption in the Z-DNA binding region of E3L reduces its pathogenicity. All these observations are important pointers towards the biological importance of Z-DNA.<ref name ='Wang'>PMID:17485386</ref> | ||
== Comparison of helix parameters of the three forms of DNA == | == Comparison of helix parameters of the three forms of DNA == | ||
