Related ArticlesBackbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
Biomol NMR Assign. 2013 Dec 24;
Authors: Peterson TA, Yu L, Piper RC
Abstract
Vps28 is one of four cytosolic proteins comprising the endosomal sorting complex required for transport I (ESCRT-I). ESCRT-I is involved in sorting ubiquitinated proteins to multivesicular bodies as well as in mediating budding of retroviruses. Here, we report the backbone and side-chain assignments of the mammalian C-terminal domain of Vps28 (mVps28(CTD)), which is involved in interactions with other ESCRT components. We also compare the predicted secondary structures of mVps28(CTD) with those of the published X-ray crystal structures of Saccharomyces cerevisiae and Xenopus laevis Vps28(CTD). These NMR resonance assignments will facilitate chemical shift mapping and structural determination of mammalian Vps28 interactions with other components of the endosomal sorting machinery that sorts ubiquitinated proteins for lysosomal degradation.
PMID: 24366722 [PubMed - as supplied by publisher]
[NMR paper] (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
Related Articles (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
Biomol NMR Assign. 2013 May 18;
Authors: Fonner BA, Tripet BP, Lui M, Zhu H, Lei B, Copié V
Abstract
Staphylococcus aureus is an opportunistic pathogen that...
nmrlearner
Journal club
0
05-21-2013 02:34 PM
[NMR paper] (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of BPSL1050 from Burkholderia pseudomallei.
(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of BPSL1050 from Burkholderia pseudomallei.
Related Articles (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of BPSL1050 from Burkholderia pseudomallei.
Biomol NMR Assign. 2013 Apr 25;
Authors: Gaudesi D, Quilici G, Musco G
Abstract
BPSL1050 is a 13.9*kDa protein produced by the Gram-negative bacterium Burkholderia pseudomallei, the etiological agent of melioidosis. Immunodetection assays against sera patients using protein microarray suggest BPSL1050...
[NMR paper] Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
Biomol NMR Assign. 2013 Jan 22;
Authors: Orbán-Németh Z, Henen MA, Geist L, Zerko S, Saxena S, Stanek J, Ko?mi?ski W, Propst F, Konrat R
Abstract
Microtubule-associated protein 1B (MAP1B) is a classical...
nmrlearner
Journal club
0
02-03-2013 10:19 AM
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Biomol NMR Assign. 2011 Jun 7;
Authors: Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we...
nmrlearner
Journal club
0
06-08-2011 11:30 AM
[NMR paper] Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic t
Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
Related Articles Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
J Biomol NMR. 2005 Apr;31(4):279-93
Authors: Gammeren AJ, Hulsbergen FB, Hollander JG, Groot HJ
This study reports the sequence specific chemical shifts...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[NMR paper] Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts
Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.
Related Articles Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.
Protein Sci. 2003 Sep;12(9):2104-8
Authors: Liu W, Rumbley J, Englander SW, Wand AJ
The mutant of horse heart cytochrome c was expressed in E. coli during growth on isotopically enriched minimal media. Complete resonance assignments of both the diamagnetic reduced (spin zero) and paramagnetic oxidized (spin (1/2))...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 doma
Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla.
Related Articles Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla.
Chembiochem. 2001 Apr 2;2(4):272-81
Authors: Pauli J, Baldus M, van Rossum B, de Groot H, Oschkinat H
The backbone and side-chain 13C and 15N signals of a solid 62-residue (u-13C,15N)-labelled protein containing the alpha-spectrin SH3 domain were...
Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
Linear Mode
