Sandbox Reserved 1122: Difference between revisions

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{{Sandbox_Reserved_ESBS_2015}}

==~~Your Heading Here (maybe something like 'Structure')~~==

==HUMAN BCL-2, ISOFORM1==

~~This~~ is ~~a default text for your page ''''''~~. ~~Click above~~ on ~~'''edit~~ this ~~page'''~~ to ~~modify. Be careful with the <~~ and ~~> signs~~.

Human BCL-2, isoform 1 is an oncoprotein of 239 residues regulating cell death (apoptosis), notably acting as an anti-apoptotic. It is encoded by the BCL2 gene located on the 18th chromosome (63.12-63.32 Mb). There are 2 isoforms of this protein (𝛼 and 𝛽), produced by alternative splicing, and which differ by 2 aminoacids (residues 96 (A←→T) and 110 (R←→G))(ref). Alteration of this protein is a caused of many cancers, and is also likely to be involved in schyzophrenia and autoimmunity.

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.

''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.''

==Primary & Secondary Structure==

Human BCL-2, isoform 1 is a 26kDa protein of 239 residues. The linear structure highlights 5 domains: BH4 (10-30), BH3 (93-107), BH1 (136-155), BH2 (187-202) and a transmembrane domain (218-239). It organizes as eight alpha-helices: from 11 to 25 (1) , from 93 to 107 (2), from 109 to 118 (3), from 126 to 137 (4), from 144-163 (5), from 169 to 184 (6), from 186 to 191 (7) and from 194 to 202(8). There are also 3 turns (32-34, 123-125, 138-140). The 3rd alpha-helix is a 3(10) helix, whereas BCL-XL 3rd helix is a normal alpha-helix.

== Function ==

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@@ Line 1: / Line 1: @@
 {{Sandbox_Reserved_ESBS_2015}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
-==Your Heading Here (maybe something like 'Structure')==
+==HUMAN BCL-2, ISOFORM1==
 <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 &lt; and &gt; signs.
+Human BCL-2, isoform 1 is an oncoprotein of 239 residues regulating cell death (apoptosis), notably acting as an anti-apoptotic. It is encoded by the BCL2 gene located on the 18th chromosome (63.12-63.32 Mb). There are 2 isoforms of this protein (𝛼 and 𝛽), produced by alternative splicing, and which differ by 2 aminoacids (residues 96 (A←→T) and 110 (R←→G))(ref). Alteration of this protein is a caused of many cancers, and is also likely to be involved in schyzophrenia and autoimmunity.
-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.
+''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.''
+==Primary & Secondary Structure==
+Human BCL-2, isoform 1 is a 26kDa protein of 239 residues. The linear structure highlights 5 domains: BH4 (10-30), BH3 (93-107), BH1 (136-155), BH2 (187-202) and a transmembrane domain (218-239). It organizes as eight alpha-helices: from 11 to 25 (1) , from 93 to 107 (2), from 109 to 118 (3), from 126 to 137 (4), from 144-163 (5), from 169 to 184 (6), from 186 to 191 (7) and from 194 to 202(8). There are also 3 turns (32-34, 123-125, 138-140). The 3rd alpha-helix is a 3(10) helix, whereas BCL-XL 3rd helix is a normal alpha-helix.
 == Function ==