Rahul Nanekar

Rahul Nanekar
  • PhD Biochemistry
  • PostDoc Position at University of Helsinki

About

15
Publications
5,256
Reads
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451
Citations
Current institution
University of Helsinki
Current position
  • PostDoc Position
Additional affiliations
December 2020 - December 2020
University of Helsinki
Position
  • PostDoc Position
September 2015 - November 2015
University of Barcelona
Position
  • EMBO
January 2010 - February 2016
University of Oulu
Position
  • PhD

Publications

Publications (15)
Article
Full-text available
Bacterial phytochrome photoreceptors usually belong to two-component signaling systems which transmit environmental stimuli to a response regulator through a histidine kinase domain. Phytochromes switch between red light-absorbing and far-red light-absorbing states. Despite exhibiting extensive structural responses during this transition, the model...
Preprint
Bacterial phytochrome photoreceptors usually belong to two-component signaling systems which transmit environmental stimuli to a response regulator through a histidine kinase domain. Phytochromes switch between red light-absorbing and far-red light-absorbing states. Despite exhibiting extensive structural responses during this transition, the model...
Article
Full-text available
Phytochrome proteins control the growth, reproduction, and photosynthesis of plants, fungi, and bacteria. Light is detected by a bilin cofactor, but it remains elusive how this leads to activation of the protein through structural changes. We present serial femtosecond X-ray crystallographic data of the chromophore-binding domains of a bacterial ph...
Preprint
Full-text available
Phytochrome proteins control the growth, reproduction, and photosynthesis of plants, fungi, and bacteria. Light is detected by a bilin cofactor, but it remains elusive how this leads to activation of the protein through structural changes. We present serial femtosecond X-ray crystallographic data of the chromophore-binding domains of a bacterial ph...
Article
Full-text available
Phytochromes are photoreceptors in plants, fungi, and various microorganisms and cycle between metastable red light-absorbing (Pr) and far-red light-absorbing (Pfr) states. Their light responses are thought to follow a conserved structural mechanism that is triggered by isomerization of the chromophore. Downstream structural changes involve refoldi...
Article
Full-text available
Membrane proteins are relatively challenging targets for structural and other biophysical studies. Insufficient expression in various expression systems, inherent flexibility, and instability in the detergents that are required for membrane extraction are the main reasons for this limited success. Therefore, identification of suitable conditions an...
Article
G-protein-coupled receptors (GPCRs) represent a major class of receptors through which a number of signals ranging from photons to large glycoprotein hormones are recognized. Human genome encodes about 800 GPCRs, yet very little structural information is available on this class of receptors. Structural studies provide a wealth of information about...
Article
The important role that extracellular adenosine plays in many physiological processes is mediated by the adenosine class of G protein-coupled receptors, a class of receptors that also responds to the antagonist caffeine, the most widely used pharmacological agent in the world. The crystallographic model of the human adenosine A(2A) receptor was rec...
Data
Titration of His-P2 with DPC, followed by intrinsic Trp fluorescence. The colouring and other details as in Figure 5C, 5D. (0.15 MB DOC)
Data
Purification of recombinant human P2. Top, gel filtration of purified P2 results in a single peak. Bottom, SDS-PAGE analysis of the fractions from the gel filtration peak indicates the expected molecular weight. (0.35 MB DOC)
Data
The N-terminal region of P2. The N terminus is shown in blue and the C terminus in red. Side chains are shown for residues 1–10, as well as the N-terminal Met residue. This region corresponds to the putative membrane-binding peptide used in the assays. (0.43 MB DOC)
Article
Full-text available
The myelin sheath is a tightly packed multilayered membrane structure insulating selected axons in the central and the peripheral nervous systems. Myelin is a biochemically unique membrane, containing a specific set of proteins. In this study, we expressed and purified recombinant human myelin P2 protein and determined its crystal structure to a re...
Article
Saltatory conduction of nerve impulses along axonal membranes depends on the presence of a multilayered membrane, myelin, that wraps around the axon. Myelin basic protein (MBP) and myelin protein 2 (P2) are intimately involved in the generation of the myelin sheath. They are also implicated in a number of neurological diseases, including autoimmune...
Article
Myelin is a multilamellar membrane which, wrapping the nerve axons, increases the efficiency of nervous signal transmission. Indeed, the molecular components of the myelin sheath interact tightly with each other and molecules on the axonal surface to drive myelination, to keep both myelin and the axon intact, and to transduce signals from myelin to...

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