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WDSPdb: a database for WD40-repeat proteins.

Wang Y, Hu XJ, Zou XD, Wu XH, Ye ZQ, Wu YD - Nucleic Acids Res. (2014)

Bottom Line: WD40-repeat proteins, as one of the largest protein families, often serve as platforms to assemble functional complexes through the hotspot residues on their domain surfaces, and thus play vital roles in many biological processes.Consequently, it is highly required for researchers who study WD40 proteins and protein-protein interactions to obtain structural information of WD40 domains.Systematic identification of WD40-repeat proteins, including prediction of their secondary structures, tertiary structures and potential hotspot residues responsible for protein-protein interactions, may constitute a valuable resource upon this request.

View Article: PubMed Central - PubMed

Affiliation: Lab of Computational Chemistry and Drug Design, Laboratory of Chemical Genomics, Peking University Shenzhen Graduate School, Shenzhen, 518055, P. R. China.

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Related in: MedlinePlus

The result page for each identified WD40-repeat protein, which comprises general annotation from UniProt database, JSmol applet presenting the predicted 3D structure and the detailed secondary structure table.
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Figure 3: The result page for each identified WD40-repeat protein, which comprises general annotation from UniProt database, JSmol applet presenting the predicted 3D structure and the detailed secondary structure table.

Mentions: The result page (Figure 3) from the database browsing or searching is composed of three parts, that is, the general annotations extracted from UniProt database, the interactive JSmol applet to present the 3D structure model and a table to show the detailed secondary structure, specific hydrogen bond network for structure stabilization and hotspot residues for PPIs. Within the structure panel of the JSmol applet, users are not only able to rotate, zoom and move the structure to get better visual angles, but also can do more sophisticated operations with the imbedded JSmol console. All of these data, including 3D structures, can be downloaded for further investigation.


WDSPdb: a database for WD40-repeat proteins.

Wang Y, Hu XJ, Zou XD, Wu XH, Ye ZQ, Wu YD - Nucleic Acids Res. (2014)

The result page for each identified WD40-repeat protein, which comprises general annotation from UniProt database, JSmol applet presenting the predicted 3D structure and the detailed secondary structure table.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4383882&req=5

Figure 3: The result page for each identified WD40-repeat protein, which comprises general annotation from UniProt database, JSmol applet presenting the predicted 3D structure and the detailed secondary structure table.
Mentions: The result page (Figure 3) from the database browsing or searching is composed of three parts, that is, the general annotations extracted from UniProt database, the interactive JSmol applet to present the 3D structure model and a table to show the detailed secondary structure, specific hydrogen bond network for structure stabilization and hotspot residues for PPIs. Within the structure panel of the JSmol applet, users are not only able to rotate, zoom and move the structure to get better visual angles, but also can do more sophisticated operations with the imbedded JSmol console. All of these data, including 3D structures, can be downloaded for further investigation.

Bottom Line: WD40-repeat proteins, as one of the largest protein families, often serve as platforms to assemble functional complexes through the hotspot residues on their domain surfaces, and thus play vital roles in many biological processes.Consequently, it is highly required for researchers who study WD40 proteins and protein-protein interactions to obtain structural information of WD40 domains.Systematic identification of WD40-repeat proteins, including prediction of their secondary structures, tertiary structures and potential hotspot residues responsible for protein-protein interactions, may constitute a valuable resource upon this request.

View Article: PubMed Central - PubMed

Affiliation: Lab of Computational Chemistry and Drug Design, Laboratory of Chemical Genomics, Peking University Shenzhen Graduate School, Shenzhen, 518055, P. R. China.

Show MeSH
Related in: MedlinePlus