1ddb

From Proteopedia

(Difference between revisions)

Revision as of 18:24, 10 March 2021

STRUCTURE OF MOUSE BID, NMR, 20 STRUCTURES

Structural highlights

1ddb is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BID_MOUSE] Induces caspases and apoptosis. Counters the protective effect of Bcl-2. The major proteolytic product p15 BID allows the release of cytochrome c.^[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

Members of the BCL2 family of proteins are key regulators of programmed cell death, acting either as apoptotic agonists or antagonists. Here we describe the solution structure of BID, presenting the structure of a proapoptotic BCL2 family member. An analysis of sequence/structure of BCL2 family members allows us to define a structural superfamily, which has implications for general mechanisms for regulating proapoptotic activity. It appears two criteria must be met for proapoptotic function within the BCL2 family: targeting of molecules to intracellular membranes, and exposure of the BH3 death domain. BID's activity is regulated by a Caspase 8-mediated cleavage event, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, resulting in a change of cellular localization.

Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists.,McDonnell JM, Fushman D, Milliman CL, Korsmeyer SJ, Cowburn D Cell. 1999 Mar 5;96(5):625-34. PMID:10089878^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gross A, Yin XM, Wang K, Wei MC, Jockel J, Milliman C, Erdjument-Bromage H, Tempst P, Korsmeyer SJ. Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death. J Biol Chem. 1999 Jan 8;274(2):1156-63. PMID:9873064
↑ McDonnell JM, Fushman D, Milliman CL, Korsmeyer SJ, Cowburn D. Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. Cell. 1999 Mar 5;96(5):625-34. PMID:10089878

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ddb"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ddb' size='340' side='right'caption='[[1ddb]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ddb]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DDB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ddb]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DDB FirstGlance]. <br>
-</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=1ddb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ddb OCA], [http://pdbe.org/1ddb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ddb RCSB], [http://www.ebi.ac.uk/pdbsum/1ddb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ddb ProSAT]</span></td></tr>
+</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=1ddb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ddb OCA], [https://pdbe.org/1ddb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ddb RCSB], [https://www.ebi.ac.uk/pdbsum/1ddb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ddb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BID_MOUSE BID_MOUSE]] Induces caspases and apoptosis. Counters the protective effect of Bcl-2. The major proteolytic product p15 BID allows the release of cytochrome c.<ref>PMID:9873064</ref>
+[[https://www.uniprot.org/uniprot/BID_MOUSE BID_MOUSE]] Induces caspases and apoptosis. Counters the protective effect of Bcl-2. The major proteolytic product p15 BID allows the release of cytochrome c.<ref>PMID:9873064</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1ddb

From Proteopedia

Revision as of 18:24, 10 March 2021

STRUCTURE OF MOUSE BID, NMR, 20 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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