mirror, a Drosophila homeobox gene in the Iroquois complex, is required for sensory organ and alula formation

Development ◽  
1998 ◽  
Vol 125 (7) ◽  
pp. 1217-1227 ◽  
Author(s):  
B.T. Kehl ◽  
K.O. Cho ◽  
K.W. Choi
Keyword(s):  
Protein Structure ◽  
Genetic Analysis ◽  
Genetic Map ◽  
Body Wall ◽  
Homeobox Gene ◽  
Structure And Function ◽  
The Other ◽  
Complex Region ◽  
Sensory Bristles ◽  
And Function

The Drosophila notum, the dorsal body wall of the thorax, is subdivided genetically into longitudinal domains (Calleja, M., Moreno, E., Pelaz, S. and Morata, G. (1996) Science 274, 252–255). Two homeobox genes clustered in the iroquois complex, araucan and caupolican, regulate proneural genes and are required for development of sensory bristles in the lateral notum (Gomez-Skarmeta, J. L., del Corral, R. D., de la Calle-Mustienes, E., Ferres-Marco, D. and Modolell, J. (1996) Cell 85, 95–105). An iroquois-related homeobox gene, mirror, was recently isolated and is localized close to the iroquois complex region (McNeil, H., Yang, C.-H., Brodsky, M., Ungos, J. and Simon, M. A. (1997) Genes and Development 11, 1073–1082; this study). We show that mirror is required for the formation of the alula and a subset of sensory bristles in the lateral domain of the notum. Genetic analysis suggests that mirror and the other iroquois genes interact to form the alula as well as the sensory organs. Based on similarities between mirror and the iroquois genes in their genetic map positions, expression, protein structure and function, mirror is considered a new member of the iroquois complex and is involved in prepatterning sensory precursor cells in the lateral notum.

PlaneFinder: a methodology to find the best plane for a set of atoms involved in the metal coordination in protein structures

2018 ◽  
Vol 51 (4) ◽  
pp. 1251-1256
Author(s):  
J. Janu Sahana ◽  
S. Sriraghav ◽  
T. A. Vijeth ◽  
T. Nagarushyanth ◽  
R. Santhosh ◽  
...  
Keyword(s):  
Protein Structure ◽  
Efficient Method ◽  
Protein Structures ◽  
Three Dimensional ◽  
Structure And Function ◽  
The Other ◽  
Metal Coordination ◽  
And Function ◽  
Interacting Atoms ◽  
Best Fit

Metal ions play a considerable role in protein structure and function. The roles of most metals and their importance are determined by the arrangements of the interacting atoms in the three-dimensional protein structure. This information is essential in predicting the geometry of the atoms involved in metal coordination. The deviation of the other atoms from the best plane is another crucial factor. The proposed web server, PlaneFinder, provides a fast and efficient method to calculate the best-fit plane for a set of atoms involved in the metal coordination. It provides in addition other possible planes by considering the maximum number of interacting atoms as well as user-selected atoms. The deviations of the selected atoms and other atoms from the best-fit plane are also displayed. PlaneFinder is freely available and can be accessed at http://bioserver1.physics.iisc.ac.in/plane/.

Order-disorder transitions of cytoplasmic N-termini in the mechanisms of P-type ATPases

2020 ◽  
Author(s):  
Khondker Rufaka Hossain ◽  
Daniel Clayton ◽  
Sophia C Goodchild ◽  
Alison Rodger ◽  
Richard James Payne ◽  
...  
Keyword(s):  
Protein Structure ◽  
Membrane Protein ◽  
Structure And Function ◽  
Membrane Protein Structure ◽  
Protein Structure And Function ◽  
Lipid Environment ◽  
Membrane Pumps ◽  
And Function ◽  
P Type

Membrane protein structure and function are modulated via interactions with their lipid environment. This is particularly true for the integral membrane pumps, the P-type ATPases. These ATPases play vital roles...

Nanoscale lipid membrane mimetics in spin-labeling and electron paramagnetic resonance spectroscopy studies of protein structure and function

2017 ◽  
Vol 6 (1) ◽  
pp. 75-92 ◽  
Author(s):  
Elka R. Georgieva
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Protein Structure ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Spin Labeling ◽  
Structure And Function ◽  
Protein Structure And Function ◽  
Paramagnetic Resonance ◽  
And Function ◽  
Electron Paramagnetic

AbstractCellular membranes and associated proteins play critical physiological roles in organisms from all life kingdoms. In many cases, malfunction of biological membranes triggered by changes in the lipid bilayer properties or membrane protein functional abnormalities lead to severe diseases. To understand in detail the processes that govern the life of cells and to control diseases, one of the major tasks in biological sciences is to learn how the membrane proteins function. To do so, a variety of biochemical and biophysical approaches have been used in molecular studies of membrane protein structure and function on the nanoscale. This review focuses on electron paramagnetic resonance with site-directed nitroxide spin-labeling (SDSL EPR), which is a rapidly expanding and powerful technique reporting on the local protein/spin-label dynamics and on large functionally important structural rearrangements. On the other hand, adequate to nanoscale study membrane mimetics have been developed and used in conjunction with SDSL EPR. Primarily, these mimetics include various liposomes, bicelles, and nanodiscs. This review provides a basic description of the EPR methods, continuous-wave and pulse, applied to spin-labeled proteins, and highlights several representative applications of EPR to liposome-, bicelle-, or nanodisc-reconstituted membrane proteins.

The deleterious impact of a non-synonymous SNP on protein structure and function is apparent in hypertension

2021 ◽  
Vol 28 (1) ◽  
Author(s):  
Kavita Sharma ◽  
Kanipakam Hema ◽  
Naveen Kumar Bhatraju ◽  
Ritushree Kukreti ◽  
Rajat Subhra Das ◽  
...  
Keyword(s):  
Protein Structure ◽  
Structure And Function ◽  
Protein Structure And Function ◽  
And Function

scholarly journals Estrogen-related Receptor β (ERRβ) – Renaissance Receptor or Receptor Renaissance?

2016 ◽  
Vol 14 (1) ◽  
pp. nrs.14002 ◽  
Author(s):  
Shailaja D. Divekar ◽  
Deanna M. Tiek ◽  
Aileen Fernandez ◽  
Rebecca B. Riggins
Keyword(s):  
Alternative Splicing ◽  
Nuclear Receptor ◽  
Family Members ◽  
Structure And Function ◽  
The Other ◽  
Orphan Nuclear Receptor ◽  
Nuclear Receptor Superfamily ◽  
And Function ◽  
The Impact ◽  
Estrogen Related Receptor

Estrogen-related receptors (ERRs) are founding members of the orphan nuclear receptor (ONR) subgroup of the nuclear receptor superfamily. Twenty-seven years of study have yet to identify cognate ligands for the ERRs, though they have firmly placed ERRα (ESRRA) and ERRγ (ESRRG) at the intersection of cellular metabolism and oncogenesis. The pace of discovery for novel functions of ERRβ (ESRRB), however, has until recently been somewhat slower than that of its family members. ERRβ has also been largely ignored in summaries and perspectives of the ONR literature. Here, we provide an overview of established and emerging knowledge of ERRβ in mouse, man, and other species, highlighting unique aspects of ERRβ biology that set it apart from the other two estrogen-related receptors, with a focus on the impact of alternative splicing on the structure and function of this receptor.

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