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| | ==NMR Structure of FAIM-CTD== | | ==NMR Structure of FAIM-CTD== |
| - | <StructureSection load='2kd2' size='340' side='right' caption='[[2kd2]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kd2' size='340' side='right'caption='[[2kd2]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kd2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KD2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kd2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KD2 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Faim, Faim1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Faim, Faim1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=2kd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kd2 OCA], [http://pdbe.org/2kd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kd2 RCSB], [http://www.ebi.ac.uk/pdbsum/2kd2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kd2 ProSAT]</span></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=2kd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kd2 OCA], [https://pdbe.org/2kd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kd2 RCSB], [https://www.ebi.ac.uk/pdbsum/2kd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kd2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FAIM1_MOUSE FAIM1_MOUSE]] Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells.<ref>PMID:10075978</ref> | + | [[https://www.uniprot.org/uniprot/FAIM1_MOUSE FAIM1_MOUSE]] Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells.<ref>PMID:10075978</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Lk3 transgenic mice]] | | [[Category: Lk3 transgenic mice]] |
| | [[Category: Hemond, M]] | | [[Category: Hemond, M]] |
| Structural highlights
Function
[FAIM1_MOUSE] Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Fas apoptosis inhibitory molecule (FAIM) is a soluble cytosolic protein inhibitor of programmed cell death and is found in organisms throughout the animal kingdom. A short isoform of FAIM is expressed in all tissue types, while an alternatively spliced long isoform is specifically expressed in the brain. Here, the short isoform is shown to consist of two independently folding domains in contact with each other. The NMR solution structure of the C-terminal domain of murine FAIM is solved in isolation and revealed to be a novel protein fold, a noninterleaved seven-stranded beta-sandwich. The structure and sequence reveal several residues that are likely to be involved in functionally significant interactions with the N-terminal domain or other binding partners. Chemical shift perturbation is used to elucidate contacts made between the N-terminal domain and the C-terminal domain.
Fas Apoptosis Inhibitory Molecule Contains a Novel beta-Sandwich in Contact with a Partially Ordered Domain.,Hemond M, Rothstein TL, Wagner G J Mol Biol. 2009 Jan 13. PMID:19168072[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schneider TJ, Fischer GM, Donohoe TJ, Colarusso TP, Rothstein TL. A novel gene coding for a Fas apoptosis inhibitory molecule (FAIM) isolated from inducibly Fas-resistant B lymphocytes. J Exp Med. 1999 Mar 15;189(6):949-56. PMID:10075978
- ↑ Hemond M, Rothstein TL, Wagner G. Fas Apoptosis Inhibitory Molecule Contains a Novel beta-Sandwich in Contact with a Partially Ordered Domain. J Mol Biol. 2009 Jan 13. PMID:19168072 doi:S0022-2836(09)00024-2
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