User:Elizabeth Cook/Sandbox 1: Difference between revisions

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Abnormal regulation of CECR2 has been linked to several diseases. It was first studied in connection with Cat Eye Syndrome, a rare congenital disorder caused by duplication of a region on chromosome 22 that includes CECR2, leading to developmental abnormalities. More recently, CECR2 has been implicated in cancer, particularly in breast cancer metastasis, where it appears to promote tumor cell invasion and immune system evasion by altering gene expression patterns. Because CECR2 influences chromatin structure and gene activity, its dysregulation can have wide-ranging effects on development, immune response, and cancer progression, making it an important target for further research and potential therapies. CECR2 is an attractive drug target because of its bromodomain, as bromodomains already have many small molecule inhibitors in use clinically.
Abnormal regulation of CECR2 has been linked to several diseases. It was first studied in connection with Cat Eye Syndrome, a rare congenital disorder caused by duplication of a region on chromosome 22 that includes CECR2, leading to developmental abnormalities. More recently, CECR2 has been implicated in cancer, particularly in breast cancer metastasis, where it appears to promote tumor cell invasion and immune system evasion by altering gene expression patterns. Because CECR2 influences chromatin structure and gene activity, its dysregulation can have wide-ranging effects on development, immune response, and cancer progression, making it an important target for further research and potential therapies. CECR2 is an attractive drug target because of its bromodomain, as bromodomains already have many small molecule inhibitors in use clinically.
In efforts to develop new small molecule inhibitors for the CECR2 bromodomain, Cpd6 has been found and studied.


[[Image:Cecr2_contacts.png|center|400px|]]
[[Image:Cecr2_contacts.png|center|400px|]]
Cpd6 makes contacts to CECR2 through N514 (2 direct H-bonds) and D464 (1 direct H-bond, and 1 H-bond coordinated by water). <ref>PMID:28740608</ref>
Cpd6 makes contacts to CECR2 through N514 (2 direct H-bonds) and D464 (1 direct H-bond, and 1 H-bond coordinated by water). <ref>PMID:28740608</ref>


The <scene name='10/1079536/Cpd6/1'>Cpd6 inhibitor</scene> is coordinated by the conserved <scene name='10/1079536/N514/1'>N514</scene> in which <scene name='10/1079536/2_bonds/1'>2 direct H-bonds</scene> form.  
In efforts to develop new small molecule inhibitors for the CECR2 bromodomain, <scene name='10/1079536/Cpd6/1'>Cpd6</scene>, an acetyllysine mimetic, has been synthesized and studied. The inhibitor is coordinated by the conserved <scene name='10/1079536/N514/1'>N514</scene> in which <scene name='10/1079536/2_bonds/1'>2 direct H-bonds</scene> form, and <scene name='10/1079536/D464/1'>D464</scene> in which there is one direct H-bond and one coordinated through water.  


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