[NMR paper] Solution NMR Structure and Histone Binding of the PHD Domain of Human MLL5.
Solution NMR Structure and Histone Binding of the PHD Domain of Human MLL5.
Related Articles Solution NMR Structure and Histone Binding of the PHD Domain of Human MLL5.
PLoS One. 2013;8(10):e77020
Authors: Lemak A, Yee A, Wu H, Yap D, Zeng H, Dombrovski L, Houliston S, Aparicio S, Arrowsmith CH
Abstract
Mixed Lineage Leukemia 5 (MLL5) is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. In addition to its catalytic domain, MLL5 contains a PHD finger domain, a protein module that...
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10-17-2013 04:57 PM
A Novel Tri-Enzyme System in Combination with Laser-Driven NMR Enables Efficient Nuclear Polarization of Biomolecules in Solution
From The DNP-NMR Blog:
A Novel Tri-Enzyme System in Combination with Laser-Driven NMR Enables Efficient Nuclear Polarization of Biomolecules in Solution
Lee, J.H. and S. Cavagnero, A Novel Tri-Enzyme System in Combination with Laser-Driven NMR Enables Efficient Nuclear Polarization of Biomolecules in Solution. The Journal of Physical Chemistry B, 2013. 117(20): p. 6069-6081.
http://dx.doi.org/10.1021/jp4010168
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07-10-2013 05:30 PM
[NMR paper] Molecular docking and NMR binding studies to identify novel inhibitors of human phosphomevalonate kinase.
Molecular docking and NMR binding studies to identify novel inhibitors of human phosphomevalonate kinase.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Molecular docking and NMR binding studies to identify novel inhibitors of human phosphomevalonate kinase.
Biochem Biophys Res Commun. 2013 Jan 4;430(1):313-9
Authors: Boonsri P, Neumann TS, Olson AL, Cai S, Herdendorf TJ, Miziorko HM, Hannongbua S, Sem DS
Abstract
Phosphomevalonate kinase (PMK)...
Solution NMR Insights into Docking Interactions Involving Inactive ERK2.
Solution NMR Insights into Docking Interactions Involving Inactive ERK2.
Solution NMR Insights into Docking Interactions Involving Inactive ERK2.
Biochemistry. 2011 Mar 30;
Authors: Piserchio A, Warthaka M, Devkota AK, Kaoud TS, Lee S, Abramczyk O, Ren P, Dalby KN, Ghose R
The mitogen activated protein (MAP) kinase ERK2 contains recruitment sites that engage canonical and non-canonical motifs found in a variety of upstream kinases, regulating phosphatases and downstream targets. Interactions involving two of these sites, the D-recruitment site...
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04-01-2011 03:51 PM
[NMR paper] Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Related Articles Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Proteins. 2005 Aug 15;60(3):367-81
Authors: van Dijk AD, Fushman D, Bonvin AM
When classical, Nuclear Overhauser Effect (NOE)-based approaches fail, it is possible, given high-resolution...
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12-01-2010 06:56 PM
[NMR paper] NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop bin
NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop binding protein.
Related Articles NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop binding protein.
RNA. 2002 Jan;8(1):83-96
Authors: DeJong ES, Marzluff WF, Nikonowicz EP
The 3' end of replication-dependent histone mRNAs terminate in a conserved sequence containing a stem-loop. This 26-nt sequence is the binding site for a protein, stem-loop binding protein (SLBP), that is involved in multiple aspects of histone mRNA metabolism...
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11-24-2010 08:49 PM
[NMR paper] Docking multiple conformations of a flexible ligand into a protein binding site using
Docking multiple conformations of a flexible ligand into a protein binding site using NMR restraints.
Related Articles Docking multiple conformations of a flexible ligand into a protein binding site using NMR restraints.
Proteins. 2002 Feb 15;46(3):295-307
Authors: Zabell AP, Post CB
A method is described for docking a large, flexible ligand using intra-ligand conformational restraints from exchange-transferred NOE (etNOE) data. Numerous conformations of the ligand are generated in isolation, and a subset of representative conformations is...
Binding Hotspots of BAZ2B Bromodomain: Histone InteractionRevealed by Solution NMR Driven Docking
Linear Mode
