Sandbox ggc16: Difference between revisions

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-==Your Heading Here (maybe something like 'Structure')==
+==(2PQ8)  '''MYST Histone Acetyltransferase'''==
-<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
+<StructureSection load='2pq8' size='340' side='right' caption='Myst Histone Acetyltransferase' scene=''>
-This is a default text for your page '''Sandbox ggc16'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
+MYST Histone Acetyltransferases (HAT), a diverse family of proteins responsible for a variety of functions in eukaryotes from yeast to humans<ref>PMID:11134336</ref>. These particular histone acetyltransferases are part of the MYST family because of their structure which includes <scene name='78/782639/Coenzyme_a/1'>coenzyme A</scene> and <scene name='78/782639/Zinc_ion/1'>Zinc Ion</scene>.
-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 ==
+Highly conserved in eukaryotes, their key roles in post-translation modification of histones. Profound effect on chromatin structure in eukaryotes. Composed of an Acetyl-CoA binding motif and a zinc finger. The enzyme looks for lysine residues which are the universal target for acetylation, and by the addition of an acetyl group stablilizes the electrons of a histone making them less positively charged.
+== Relevance ==
+These enzymes acetylate lysine amino acids of histone by transferring the acetyl group of acetyl CoA to form N-acetyllysine. While the DNA coiled around histones and the activity of histone acetyltransferase is able to turn genes on or off, along with influencing gene expression by acetylating non-histone proteins<ref>PMID:10441070</ref>.
 == Disease ==
+HATs activate the residues of p53 by acetylation which leads to the elevation of p53 DNA binding or loss of its transcriptional activity<ref>PMID:10441070</ref>. If there’s any type of mutation where acetylation occurs of the p53 residues the functionality is hindered leading to the growth of tumors/cancers.
-== Relevance ==
 == Structural highlights ==
-{{Template:ColorKey_N52C3Rainbow}}<scene name='78/782639/N_to_c_rainbow/1'>N to C Sequence</scene>
+The binding site for this structure <scene name='78/782639/Coenzyme_a/3'>coenzyme A</scene>, which is involved in the transfer of an acetyl group from acetyl-CoA to the amine group of a lysine residue. The <scene name='78/782639/Zinc_ion/1'>zinc</scene> finger region of this structure is involved in the acetyltransferase activity and chromatin binding of the histone. The <scene name='78/782639/Cysteine_rich_structure/1'>cysteine</scene> residues are needed for catalyzing specific acetylation.
 </StructureSection>
 == References ==
 <references/>
+<ref>PMID:11134336</ref>
+<ref><ref>DOI: 10.1021/acschembio.5b00841</ref>PMID:11057899</ref>