Structural Characterization of Protein–Protein Interactions with pyDockSAXS
Structural characterization of protein–protein interactions can provide essential details to understand biological functions at the molecular level and to facilitate their manipulation for biotechnological and biomedical purposes. Unfortunately, the 3D structure is available for only a small fraction of all possible protein–protein interactions, due to the technical limitations of high-resolution structural determination methods. In this context, low-resolution structural techniques, such as small-angle X-ray scattering (SAXS), can be combined with computational docking to provide structural models of protein–protein interactions at large scale. In this chapter, we describe the pyDockSAXS web server (https://life.bsc.es/pid/pydocksaxs), which uses pyDock docking and scoring to provide structural models that optimally satisfy the input SAXS data. This server, which is freely available to the scientific community, provides an automatic pipeline to model the structure of a protein–protein complex from SAXS data.
Main Authors: | , , |
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Other Authors: | |
Format: | capítulo de libro biblioteca |
Language: | English |
Published: |
Springer Nature
2020
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Subjects: | Protein–protein interactions, Structural modeling, Small-angle X-ray scattering (SAXS), Computational docking, FTDock, CRYSOL, pyDock, |
Online Access: | http://hdl.handle.net/10261/232368 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/501100001665 |
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