KKT4 is a multi-domain kinetochore protein specific to kinetoplastids, such as Trypanosoma brucei. It lacks significant sequence similarity to known kinetochore proteins in other eukaryotes. Our recent X-ray structure of the C-terminal region of KKT4 shows that it has a tandem BRCT (BRCA1 C Terminus) domain fold with a sulfate ion bound in a typical binding site for a phosphorylated serine or threonine. Here we present the ¹H, ^(13)C and ^(15)N resonance assignments for the BRCT domain of KKT4...
[NMR paper] NMR Methods to Study the Dynamics of SH2 Domain-Phosphopeptide Complexes
NMR Methods to Study the Dynamics of SH2 Domain-Phosphopeptide Complexes
Nuclear magnetic resonance (NMR) spectroscopy is the method of choice for studying the dynamics of biological macromolecules in solution. By exploiting the intricate interplay between the effects of protein motion (both overall rotational diffusion and internal mobility) and nuclear spin relaxation, NMR allows molecular motion to be probed at atomic resolution over a wide range of timescales, including picosecond (bond vibrations and methyl-group rotations), nanosecond (loop motions and...
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[NMR paper] 19F NMR as a versatile tool to study (membrane) protein structure and dynamics.
19F NMR as a versatile tool to study (membrane) protein structure and dynamics.
Related Articles 19F NMR as a versatile tool to study (membrane) protein structure and dynamics.
Biol Chem. 2018 Dec 01;:
Authors: Rose-Sperling D, Tran MA, Lauth LM, Goretzki B, Hellmich UA
Abstract
To elucidate the structures and dynamics of membrane proteins, highly advanced biophysical methods have been developed that often require significant resources, both for sample preparation and experimental analyses. For very complex systems, such as...
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Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein
Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein
Publication date: 27 February 2018
Source:Biophysical Journal, Volume 114, Issue 4</br>
Author(s): Karl T. Debiec, Matthew J. Whitley, Leonardus M.I. Koharudin, Lillian T. Chong, Angela M. Gronenborn</br>
Multidomain proteins with two or more independently folded functional domains are prevalent in nature. Whereas most multidomain proteins are linked linearly in sequence, roughly one-tenth possess domain insertions where a guest domain is implanted into a loop...
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[NMR paper] Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein.
Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein.
Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein.
Biophys J. 2018 Feb 27;114(4):839-855
Authors: Debiec KT, Whitley MJ, Koharudin LMI, Chong LT, Gronenborn AM
Abstract
Multidomain proteins with two or more independently folded functional domains are prevalent in nature. Whereas most multidomain proteins are linked linearly in sequence, roughly one-tenth possess domain insertions where...
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[NMR paper] NMR Mapping of PCNA Interaction with Translesion Synthesis DNA Polymerase Rev1 Mediated by Rev1-BRCT Domain.
NMR Mapping of PCNA Interaction with Translesion Synthesis DNA Polymerase Rev1 Mediated by Rev1-BRCT Domain.
Related Articles NMR Mapping of PCNA Interaction with Translesion Synthesis DNA Polymerase Rev1 Mediated by Rev1-BRCT Domain.
J Mol Biol. 2013 Jun 6;
Authors: Pustovalova Y, Maciejewski MW, Korzhnev DM
Abstract
Rev1 is a Y-family translesion synthesis (TLS) DNA polymerase involved in bypass replication across sites of DNA damage and postreplicational gap filling. In the process of TLS high-fidelity replicative DNA polymerases...
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[NMR paper] NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein
NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
Biochemistry. 1997 Sep 2;36(35):10709-17
Authors: Xu RX, Pawelczyk T, Xia TH, Brown SC
Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich...
NMR study of the structure and dynamics of the BRCT domain from the kinetochore protein KKT4
Linear Mode
