Results 211 to 220 of about 22,091 (247)

Domain swapping in the sporulation response regulator Spo0A

Journal of Molecular Biology, 2000
Adaptive responses of micro-organisms, such as chemotaxis and sporulation, are governed by two-component systems consisting of sensor kinases, that interpret environmental signals, and response regulators which activate the appropriate physiological responses.
Gordon Leonard, James Brannigan, Wanda Lewis   +2 more
exaly   +3 more sources

Sequence-structure Signals of 3D Domain Swapping in Proteins

Journal of Molecular Biology, 2003
Three-dimensional domain swapping occurs when two or more identical proteins exchange identical parts of their structure to generate an oligomeric unit. It affects proteins with diverse sequences and structures, and is expected to play important roles in evolution, functional regulation and even conformational diseases.
Dimitri Gilis, Marianne Rooman, Christophe Biot   +2 more
exaly   +4 more sources

Domain swapping of death domain superfamily: Alternative strategy for dimerization

International Journal of Biological Macromolecules, 2019
The role of death domain (DD) protein-mediated inter-protein interactions in cell death and immune cell signaling have been extensively investigated as they are tentative targets for therapeutic interventions and are involved in signal transduction. Structural studies, especially those involving the recent advanced cryo-electron microscopy, indicated ...
Hyun Ho Park
exaly   +3 more sources

Domain swapping in materials design

Peptide Science, 2010
AbstractPeptide self‐assembly can be used as a bottom–up approach to material fabrication. Although many different types of materials can be prepared from peptides, hydrogels are perhaps one of the most common. Gels typically result from the self‐assembly of peptides into fibrillar networks.
Radhika P, Nagarkar, Rohan A, Hule, Darrin J, Pochan, Joel P, Schneider   +3 more
openaire   +2 more sources

Protein Reconstitution and 3D Domain Swapping

Current Protein & Peptide Science, 2002
The native structures of proteins are governed by a large number of non-covalent interactions yielding a high specificity for the native packing of structural elements. This allows for the reconstitution of proteins from disconnected polypeptide fragments.
Maria, Håkansson, Sara, Linse
openaire   +2 more sources

A kinetic study of domain swapping of Protein L

Physical Chemistry Chemical Physics, 2014
Domain swapping of the B1 domain of Protein L isolated from Peptostreptococcus magnus can be induced by rational mutation. We show that the monomeric and the domain swapped dimeric forms of the G55A mutant of Protein L are directly observable by solution NMR spectroscopy under equilibrium conditions.
Thomas, Moschen, Martin, Tollinger
openaire   +2 more sources

Domain Swapping in the Human Histamine H1 Receptor

The Journal of Pharmacology and Experimental Therapeutics, 2004
G-protein-coupled receptors (GPCRs) represent the largest family of receptors involved in transmembrane signaling. Although these receptors were generally believed to be monomeric entities, accumulating evidence supports the presence of GPCRs in multimeric forms.
Bakker, R.A., Dees, G., Carrillo, J.J., Booth, R.G., Lopez-Gimenez, J.F., Milligan, G., Strange, P.G., Leurs, R.   +7 more
openaire   +2 more sources

Evolution of protein function by Domain swapping

2001
Publisher Summary This chapter explores the use of large exchanges of structure (subdomains, domains, and whole proteins) to evolve new function in proteins. These include the formation of multifunctional proteins, tandem duplication, domain recruitment, and circular permutation.
M, Ostermeier, S J, Benkovic
openaire   +2 more sources

Domain Swapping in the Cytoplasmic Domain of the Escherichia coli Rhomboid Protease

Journal of Molecular Biology, 2013
Rhomboids are membrane-embedded serine proteases that cleave membrane protein substrates. Escherichia coli rhomboid GlpG (ecGlpG) consists of an N-terminal cytoplasmic domain and a membrane domain containing the active site. We determined the crystal structure of the soluble cytoplasmic domain of ecGlpG at 1.35Å resolution and examined whether this ...
Christelle, Lazareno-Saez, Elena, Arutyunova, Nicolas, Coquelle, M Joanne, Lemieux   +3 more
openaire   +2 more sources

Domain swapping of CD4 upon dimerization

Proteins: Structure, Function, and Bioinformatics, 2004
AbstractIt has recently been shown that disulfide bond Cys130—Cys159 in domain 2 of monomeric CD4 is involved in the formation of CD4 disulfide‐bonded dimers on cell surfaces and that it can influence the permissiveness of cells to HIV infection. Because this disulfide bond is buried in the monomer, a large conformational change must take place in ...
openaire   +3 more sources