schliessen

Filtern

 

Bibliotheken

High-definition NMR structure of PED/PEA-15 death effector domain reveals details of key polar side chain interactions.

Highlights► We refine a solution NMR structure of the death effector domain of PED/PEA-15. ► Structure refinement involves dual-medium RDCs and explicit solvent protocol. ► Refined structure possesses higher quality comparing to existing structure. ► Functionally crucial polar interactions are ident... Full description

Journal Title: Biochemical and biophysical research communications July 20, 2012, Vol.424(1), pp.141-146
Main Author: Twomey, Edward C
Other Authors: Wei, Yufeng
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1090-2104 ; DOI: 1090-2104 ; DOI: 10.1016/j.bbrc.2012.06.091
Link: http://search.proquest.com/docview/1027683056/?pq-origsite=primo
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: proquest1027683056
title: High-definition NMR structure of PED/PEA-15 death effector domain reveals details of key polar side chain interactions.
format: Article
creator:
  • Twomey, Edward C
  • Wei, Yufeng
subjects:
  • Humans–Chemistry
  • Intracellular Signaling Peptides and Proteins–Chemistry
  • Nuclear Magnetic Resonance, Biomolecular–Chemistry
  • Phosphoproteins–Chemistry
  • Protein Structure, Tertiary–Chemistry
  • Intracellular Signaling Peptides and Proteins
  • Pea15 Protein, Human
  • Phosphoproteins
ispartof: Biochemical and biophysical research communications, July 20, 2012, Vol.424(1), pp.141-146
description: Highlights► We refine a solution NMR structure of the death effector domain of PED/PEA-15. ► Structure refinement involves dual-medium RDCs and explicit solvent protocol. ► Refined structure possesses higher quality comparing to existing structure. ► Functionally crucial polar interactions are identified in refined structure. Death effector domain (DED) proteins constitute a subfamily of the large death domain superfamily that is primarily involved in apoptosis pathways. DED structures have characteristic side chain–side chain interactions among polar residues on the protein surface, forming a network of hydrogen bonds and salt bridges. The polar interaction network is functionally important in promoting protein–protein interactions by maintaining optimal side chain orientations. We have refined the solution DED structure of the PED/PEA-15 protein, a representative member of DED subfamily, using traditional NMR restraints with the addition of residual dipolar coupling (RDC) restraints from two independent alignment media, and employed the explicit solvent refinement protocol. The newly refined DED structure of PED/PEA-15 possesses higher structural quality as indicated by WHAT IF Z-scores, with most significant improvement in the backbone conformation normality quality factor. This higher quality DED structure of PED/PEA-15 leads to the identification of a number of key polar side chain interactions, which are not typically observed in NMR protein structures. The elucidation of polar side chain interactions is a key step towards the understanding of protein–protein interactions involving the death domain superfamily. The NMR structures with extensive details of protein structural features are thereby termed high-definition (HD) NMR structures.
language: eng
source:
identifier: E-ISSN: 1090-2104 ; DOI: 1090-2104 ; DOI: 10.1016/j.bbrc.2012.06.091
fulltext: fulltext
issn:
  • 10902104
  • 1090-2104
url: Link


@attributes
ID1606275633
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid1027683056
sourceidproquest
recordidTN_proquest1027683056
sourcesystemOther
pqid1027683056
galeid297202659
display
typearticle
titleHigh-definition NMR structure of PED/PEA-15 death effector domain reveals details of key polar side chain interactions.
creatorTwomey, Edward C ; Wei, Yufeng
contributorTwomey, Edward C (correspondence author) ; Twomey, Edward C (record owner)
ispartofBiochemical and biophysical research communications, July 20, 2012, Vol.424(1), pp.141-146
identifier
subjectHumans–Chemistry ; Intracellular Signaling Peptides and Proteins–Chemistry ; Nuclear Magnetic Resonance, Biomolecular–Chemistry ; Phosphoproteins–Chemistry ; Protein Structure, Tertiary–Chemistry ; Intracellular Signaling Peptides and Proteins ; Pea15 Protein, Human ; Phosphoproteins
languageeng
source
descriptionHighlights► We refine a solution NMR structure of the death effector domain of PED/PEA-15. ► Structure refinement involves dual-medium RDCs and explicit solvent protocol. ► Refined structure possesses higher quality comparing to existing structure. ► Functionally crucial polar interactions are identified in refined structure. Death effector domain (DED) proteins constitute a subfamily of the large death domain superfamily that is primarily involved in apoptosis pathways. DED structures have characteristic side chain–side chain interactions among polar residues on the protein surface, forming a network of hydrogen bonds and salt bridges. The polar interaction network is functionally important in promoting protein–protein interactions by maintaining optimal side chain orientations. We have refined the solution DED structure of the PED/PEA-15 protein, a representative member of DED subfamily, using traditional NMR restraints with the addition of residual dipolar coupling (RDC) restraints from two independent alignment media, and employed the explicit solvent refinement protocol. The newly refined DED structure of PED/PEA-15 possesses higher structural quality as indicated by WHAT IF Z-scores, with most significant improvement in the backbone conformation normality quality factor. This higher quality DED structure of PED/PEA-15 leads to the identification of a number of key polar side chain interactions, which are not typically observed in NMR protein structures. The elucidation of polar side chain interactions is a key step towards the understanding of protein–protein interactions involving the death domain superfamily. The NMR structures with extensive details of protein structural features are thereby termed high-definition (HD) NMR structures.
version5
lds50peer_reviewed
links
openurl$$Topenurl_article
openurlfulltext$$Topenurlfull_article
backlink$$Uhttp://search.proquest.com/docview/1027683056/?pq-origsite=primo$$EView_record_in_ProQuest_(subscribers_only)
search
creatorcontrib
0Twomey, Edward C
1Wei, Yufeng
titleHigh-definition NMR structure of PED/PEA-15 death effector domain reveals details of key polar side chain interactions.
subject
0Humans–Chemistry
1Intracellular Signaling Peptides and Proteins–Chemistry
2Nuclear Magnetic Resonance, Biomolecular–Chemistry
3Phosphoproteins–Chemistry
4Protein Structure, Tertiary–Chemistry
5Intracellular Signaling Peptides and Proteins
6Pea15 Protein, Human
7Phosphoproteins
82LS7
9PDB
general
0English
11090-2104
210.1016/j.bbrc.2012.06.091
3MEDLINE (ProQuest)
4ProQuest Biological Science Collection
5ProQuest Natural Science Collection
6ProQuest SciTech Collection
7Biological Science Database
8Natural Science Collection
9SciTech Premium Collection
10Health Research Premium Collection
11Health Research Premium Collection (Alumni edition)
sourceidproquest
recordidproquest1027683056
issn
010902104
11090-2104
rsrctypearticle
creationdate2012
addtitleBiochemical and biophysical research communications
searchscope
01007527
11007944
210000004
310000038
410000050
510000120
610000159
710000238
810000253
910000260
1010000270
1110000271
1210000302
13proquest
scope
01007527
11007944
210000004
310000038
410000050
510000120
610000159
710000238
810000253
910000260
1010000270
1110000271
1210000302
13proquest
lsr43
01007527false
11007944false
210000004false
310000038false
410000050false
510000120false
610000159false
710000238false
810000253false
910000260false
1010000270false
1110000271false
1210000302false
contributorTwomey, Edward C
startdate20120720
enddate20120720
citationpf 141 pt 146 vol 424 issue 1
lsr30VSR-Enriched:[description, galeid, issn, pqid]
sort
titleHigh-definition NMR structure of PED/PEA-15 death effector domain reveals details of key polar side chain interactions.
authorTwomey, Edward C ; Wei, Yufeng
creationdate20120720
lso0120120720
facets
frbrgroupid7490383042340069892
frbrtype5
newrecords20181218
languageeng
creationdate2012
topic
0Humans–Chemistry
1Intracellular Signaling Peptides and Proteins–Chemistry
2Nuclear Magnetic Resonance, Biomolecular–Chemistry
3Phosphoproteins–Chemistry
4Protein Structure, Tertiary–Chemistry
5Intracellular Signaling Peptides and Proteins
6Pea15 Protein, Human
7Phosphoproteins
collection
0MEDLINE (ProQuest)
1ProQuest Biological Science Collection
2ProQuest Natural Science Collection
3ProQuest SciTech Collection
4Biological Science Database
5Natural Science Collection
6SciTech Premium Collection
7Health Research Premium Collection
8Health Research Premium Collection (Alumni edition)
prefilterarticles
rsrctypearticles
creatorcontrib
0Twomey, Edward C
1Wei, Yufeng
jtitleBiochemical and biophysical research communications
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextfulltext
addata
aulast
0Twomey
1Wei
aufirst
0Edward C
1Yufeng
au
0Twomey, Edward C
1Wei, Yufeng
addauTwomey, Edward C
atitleHigh-definition NMR structure of PED/PEA-15 death effector domain reveals details of key polar side chain interactions.
jtitleBiochemical and biophysical research communications
risdate20120720
volume424
issue1
spage141
epage146
pages141-146
eissn1090-2104
formatjournal
genrearticle
ristypeJOUR
doi10.1016/j.bbrc.2012.06.091
urlhttp://search.proquest.com/docview/1027683056/
issn0006291X
date2012-07-20