3i1h
From Proteopedia
(Difference between revisions)
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<StructureSection load='3i1h' size='340' side='right' caption='[[3i1h]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='3i1h' size='340' side='right' caption='[[3i1h]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3i1h]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I1H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I1H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3i1h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I1H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I1H FirstGlance]. <br> |
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCL2A1, BCL2L5, BFL1, GRS, HBPA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3i1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i1h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i1h RCSB], [http://www.ebi.ac.uk/pdbsum/3i1h PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3i1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i1h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i1h RCSB], [http://www.ebi.ac.uk/pdbsum/3i1h PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/B2LA1_HUMAN B2LA1_HUMAN]] Retards apoptosis induced by IL-3 deprivation. May function in the response of hemopoietic cells to external signals and in maintaining endothelial survival during infection (By similarity). [[http://www.uniprot.org/uniprot/BAK_HUMAN BAK_HUMAN]] In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 or its adenovirus homolog E1B 19k protein. Low micromolar levels of zinc ions inhibit the promotion of apoptosis.<ref>PMID:8521816</ref> <ref>PMID:17157251</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Bcl-2|Bcl-2]] | *[[Bcl-2|Bcl-2]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Acton, T]] | [[Category: Acton, T]] | ||
[[Category: Gelinas, C]] | [[Category: Gelinas, C]] | ||
Revision as of 06:21, 25 December 2014
Crystal structure of human BFL-1 in complex with BAK BH3 peptide
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Categories: Human | Acton, T | Gelinas, C | Guan, R | Montelione, G T | Structural genomic | White, E | Xiao, R | Zhao, L | Apoptosis | Bak bh3 | Bcl-2 family | Bfl-1 | Complex | Membrane | Metal-binding | Nesg | Pro-survival protein | PSI, Protein structure initiative | Transmembrane
