Results 241 to 250 of about 169,270 (280)

Natural-like function in artificial WW domains

Nature, 2005
Protein sequences evolve through random mutagenesis with selection for optimal fitness. Cooperative folding into a stable tertiary structure is one aspect of fitness, but evolutionary selection ultimately operates on function, not on structure. In the accompanying paper, we proposed a model for the evolutionary constraint on a small protein interaction
William P, Russ, Drew M, Lowery, Prashant, Mishra, Michael B, Yaffe, Rama, Ranganathan   +4 more
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A map of WW domain family interactions

PROTEOMICS, 2004
Abstract WW domains are protein modules that bind proline‐rich ligands. WW domain‐ligand complexes are of importance as they have been implicated in several human diseases such as muscular dystrophy, cancer, hypertension, Alzheimer's, and Huntington's diseases. We report the results of a protein array aimed at mapping all the human WW
Hai, Hu, John, Columbus, Yi, Zhang, Dongying, Wu, Lubing, Lian, Song, Yang, Jennifer, Goodwin, Christine, Luczak, Mark, Carter, Lin, Chen, Michael, James, Roger, Davis, Marius, Sudol, John, Rodwell, Juan J, Herrero   +14 more
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WW domain-containing oxidoreductase: a candidate tumor suppressor

Trends in Molecular Medicine, 2007
Common fragile site gene WWOX encodes a candidate tumor suppressor WW domain-containing oxidoreductase. Alteration of this gene, along with dramatic downregulation of WWOX protein, is shown in the majority of invasive cancer cells. Ectopic WWOX exhibits proapoptotic and tumor inhibitory functions in vitro and in vivo, probably interacting with growth ...
Nan-Shan, Chang, Li-Jin, Hsu, Yee-Shin, Lin, Feng-Jie, Lai, Hamm-Ming, Sheu   +4 more
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Structural characterisation of PinA WW domain and a comparison with other Group IV WW domains, Pin1 and Ess1

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2008
The NMR solution structure of the PinA WW domain from Aspergillus nidulans is presented. The backbone of the PinA WW domain is composed of a triple-stranded anti-parallel beta-sheet and an alpha-helix similar to Ess1 and Pin1 without the alpha-helix linker. Large RMS deviations in Loop I were observed both from the NMR structures and molecular dynamics
Ng, Chai Ann., Kato, Yusuke., Tanokura, Masaru., Brownlee, Robert T. C.   +3 more
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WW (WWP) Domains: From Structure to Function

1998
The WW domain, also known as WWP, or rsp5 domain, is a ~40 amino acid module which was identified in late 1994 by three different groups (Bork and Sudol 1994; Andre and Springael 1994; Hofmann and Bucher 1995). The name WW or WWP is based on the primary sequence of the domain, which includes two highly conserved tryptophans and an invariant proline ...
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Structural analysis of WW domains and design of a WW prototype.

Nature structural biology, 2000
Two new NMR structures of WW domains, the mouse formin binding protein and a putative 84.5 kDa protein from Saccharomyces cerevisiae, show that this domain, only 35 amino acids in length, defines the smallest monomeric triple-stranded antiparallel beta-sheet protein domain that is stable in the absence of disulfide bonds, tightly bound ions or ligands.
M J, Macias, V, Gervais, C, Civera, H, Oschkinat   +3 more
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Sequence-specific dynamics modulate recognition specificity in WW domains

Nature Structural & Molecular Biology, 2007
The current canon attributes the binding specificity of protein-recognition motifs to distinctive chemical moieties in their constituent amino acid sequences. However, we show for a WW domain that the sequence crucial for specificity is an intrinsically flexible loop that partially rigidifies upon ligand docking.
Tao, Peng, John S, Zintsmaster, Andrew T, Namanja, Jeffrey W, Peng   +3 more
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Characterization of KIBRA, a novel WW domain-containing protein

Biochemical and Biophysical Research Communications, 2003
In a yeast two hybrid screen with the human isoform of Dendrin (KIAA0749), a putative modulator of the postsynaptic cytoskeleton, we isolated a cDNA coding for a novel protein, KIBRA, possessing two amino-terminal WW domains, an internal C2-like domain and a carboxy-terminal glutamic acid-rich stretch.
Joachim, Kremerskothen, Christian, Plaas, Katrin, Büther, Indra, Finger, Stefan, Veltel, Theodoros, Matanis, Thomas, Liedtke, Angelika, Barnekow   +7 more
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WW domains and retrovirus budding

Nature, 1996
L, Garnier, J W, Wills, M F, Verderame, M, Sudol   +3 more
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