1gjh: Difference between revisions

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-[[Image:1gjh.png|left|200px]]
-<!--
+==HUMAN BCL-2, ISOFORM 2==
-The line below this paragraph, containing "STRUCTURE_1gjh", creates the "Structure Box" on the page.
+<StructureSection load='1gjh' size='340' side='right'caption='[[1gjh]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1gjh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1g5o 1g5o]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GJH FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjh OCA], [https://pdbe.org/1gjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gjh RCSB], [https://www.ebi.ac.uk/pdbsum/1gjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjh ProSAT]</span></td></tr>
-{{STRUCTURE_1gjh|  PDB=1gjh  |  SCENE=  }}
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/BCL2_HUMAN BCL2_HUMAN] Note=A chromosomal aberration involving BCL2 has been found in chronic lymphatic leukemia. Translocation t(14;18)(q32;q21) with immunoglobulin gene regions. BCL2 mutations found in non-Hodgkin lymphomas carrying the chromosomal translocation could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions.
+== Function ==
+[https://www.uniprot.org/uniprot/BCL2_HUMAN BCL2_HUMAN] Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1).<ref>PMID:18570871</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gj/1gjh_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gjh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The structures of two isoforms of Bcl-2 that differ by two amino acids have been determined by NMR spectroscopy. Because wild-type Bcl-2 behaved poorly in solution, the structures were determined by using Bcl-2/Bcl-x(L) chimeras in which part of the putative unstructured loop of Bcl-2 was replaced with a shortened loop from Bcl-x(L). These chimeric proteins have a low pI compared with the wild-type protein and are soluble. The structures of the two Bcl-2 isoforms consist of 6 alpha-helices with a hydrophobic groove on the surface similar to that observed for the homologous protein, Bcl-x(L). Comparison of the Bcl-2 structures to that of Bcl-x(L) shows that although the overall fold is the same, there are differences in the structural topology and electrostatic potential of the binding groove. Although the structures of the two isoforms of Bcl-2 are virtually identical, differences were observed in the ability of the proteins to bind to a 25-residue peptide from the proapoptotic Bad protein and a 16-residue peptide from the proapoptotic Bak protein. These results suggest that there are subtle differences in the hydrophobic binding groove in Bcl-2 that may translate into differences in antiapoptotic activity for the two isoforms.
-===HUMAN BCL-2, ISOFORM 2===
+Solution structure of the antiapoptotic protein bcl-2.,Petros AM, Medek A, Nettesheim DG, Kim DH, Yoon HS, Swift K, Matayoshi ED, Oltersdorf T, Fesik SW Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3012-7. Epub 2001 Feb 27. PMID:11248023<ref>PMID:11248023</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1gjh" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_11248023}}, adds the Publication Abstract to the page
+*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 11248023 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11248023}}
+__TOC__
+</StructureSection>
-==About this Structure==
-[[1gjh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1g5o 1g5o]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJH OCA].
-==Reference==
-<ref group="xtra">PMID:11248023</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Fesik, S W.]]
+[[Category: Large Structures]]
-[[Category: Kim, D H.]]
+[[Category: Fesik SW]]
-[[Category: Matayoshi, E D.]]
+[[Category: Kim DH]]
-[[Category: Medek, A.]]
+[[Category: Matayoshi ED]]
-[[Category: Nettesheim, D G.]]
+[[Category: Medek A]]
-[[Category: Oltersdorf, T.]]
+[[Category: Nettesheim DG]]
-[[Category: Petros, A M.]]
+[[Category: Oltersdorf T]]
-[[Category: Swift, K.]]
+[[Category: Petros AM]]
-[[Category: Yoon, H S.]]
+[[Category: Swift K]]
-[[Category: Apoptosis]]
+[[Category: Yoon HS]]