Daniel Nietlispach

We report here the 1 H, 15 N and 13 C resonance assignments for the small G protein RalB bound to the GTP analogue, GMPPNP and complexed with the Ral binding domain of its downstream effector RLIP76. The BMRB accession code is 15525.

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1H, 13C, and 15N resonance assignments for the small G protein RalB in its active conformation

Biomolecular NMR Assignments (2007)

Sunil Prasannan R. Bryn Fenwick Louise J. Campbell Katrina A. Evetts Daniel Nietlispach

Amide

Protein Dynamics

10.1007/s12104-007-9040-1

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Solution structure of the apo state of the acyl carrier protein from the MLSA2 subunit of the mycolactone polyketide synthase

Steven Vance О. В. Ткаченко B. K. Thomas M. Bassuni Hui Hong

Acyl carrier protein

Polyketide synthase

10.2210/pdb5hvc/pdb

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1H, 13C and 15N resonance assignments of the Cdc42-binding domain of TOCA1

Biomolecular NMR Assignments (2016)

Joanna R. Watson Daniel Nietlispach Darerca Owen Helen R. Mott

TOCA1 is a downstream effector protein of the small GTPase, Cdc42. It is a multi-domain protein that includes a membrane binding F-BAR domain, a homology region 1 (HR1) domain, which binds selectively to active Cdc42 and an SH3 domain. TOCA1 is involved in the regulation of actin dynamics in processes such as endocytosis, filopodia formation, neurite elongation, cell motility and invasion. Structural insight into the interaction between TOCA1 and Cdc42 will contribute to our understanding of the role of TOCA1 in actin dynamics. The (1)H, (15)N and (13)C NMR backbone and sidechain resonance assignment of the HR1 domain (12 kDa) presented here provides the foundation for structural studies of the domain and its interactions.

CDC42

Filopodia

Small GTPase

10.1007/s12104-016-9677-8

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An Approach to the Structure Determination of Larger Proteins Using Triple Resonance NMR Experiments in Conjunction with Random Fractional Deuteration

Journal of the American Chemical Society (1996)

Daniel Nietlispach Robin T Clowes R. William Broadhurst Yutaka Ito James Keeler

A combination of simulation and experiment is used to demonstrate that the sensitivity of a family of 3D/4D NMR experiments used to assign resonances and to obtain structural restraints in proteins is improved by partial random deuteration; the improvement increases as the correlation time of the protein becomes longer. The results suggest that deuteration at a level of ∼50% optimizes the sensitivity of experiments which are used to assign sidechain 1H and 13C resonances by correlating them with the resonances from backbone nuclei. In addition, this level of deuteration is also a good compromise for recording NOESY experiments. Using this approach, it should be possible to determine structures of larger proteins.

10.1021/ja952207b

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Citations (113)

Daniel Nietlispach

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