This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1ibx

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 14:25, 27 October 2021

NMR STRUCTURE OF DFF40 AND DFF45 N-TERMINAL DOMAIN COMPLEX

Structural highlights

1ibx is a 2 chain structure with sequence from Human and Strsp. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	DFF40 (HUMAN), DFF45 (STRSP)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DFFB_HUMAN] Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.

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

Apoptotic DNA fragmentation is mediated by a caspase-activated DNA fragmentation factor (DFF)40. Expression and folding of DFF40 require the presence of DFF45, which also acts as a nuclease inhibitor before DFF40 activation by execution caspases. The N-terminal domains (NTDs) of both proteins are homologous, and their interaction plays a key role in the proper functioning of this two-component system. Here we report that the NTD of DFF45 alone is unstructured in solution, and its folding is induced upon binding to DFF40 NTD. Therefore, folding of both proteins regulates the formation of the DFF40/DFF45 complex. The solution structure of the heterodimeric complex between NTDs of DFF40 and DFF45 reported here shows that the mutual chaperoning includes the formation of an extensive network of intermolecular interactions that bury a hydrophobic cluster inside the interface, surrounded by intermolecular salt bridges.

Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45.,Zhou P, Lugovskoy AA, McCarty JS, Li P, Wagner G Proc Natl Acad Sci U S A. 2001 May 22;98(11):6051-5. PMID:11371636^[1]

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

References

↑ Zhou P, Lugovskoy AA, McCarty JS, Li P, Wagner G. Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6051-5. PMID:11371636 doi:10.1073/pnas.111145098

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/1ibx"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ibx' size='340' side='right'caption='[[1ibx]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ibx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Strsp Strsp]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1IBX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ibx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Strsp Strsp]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IBX FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DFF40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DFF45 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1306 STRSP])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DFF40 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DFF45 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1306 STRSP])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ibx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibx OCA], [http://pdbe.org/1ibx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ibx RCSB], [http://www.ebi.ac.uk/pdbsum/1ibx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ibx 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=1ibx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibx OCA], [https://pdbe.org/1ibx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ibx RCSB], [https://www.ebi.ac.uk/pdbsum/1ibx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ibx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DFFB_HUMAN DFFB_HUMAN]] Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.
+[[https://www.uniprot.org/uniprot/DFFB_HUMAN DFFB_HUMAN]] Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1ibx

From Proteopedia

Revision as of 14:25, 27 October 2021

NMR STRUCTURE OF DFF40 AND DFF45 N-TERMINAL DOMAIN COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox