FoXS, FoXSDock and MultiFoXS: Single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles

被引：373

作者：

Schneidman-Duhovny, Dina ^{[1
,2
]}

Hammel, Michal ^{[3
]}

Tainer, John A. ^{[3
,4
]}

Sali, Andrej ^{[1
,2
]}

机构：

[1] Univ Calif San Francisco, Dept Pharmaceut Chem, Dept Bioengn & Therapeut Sci, San Francisco, CA 94143 USA

[2] Univ Calif San Francisco, Calif Inst Quantitat Biosci QB3, San Francisco, CA 94143 USA

[3] Lawrence Berkeley Natl Lab, Mol Biophys & Integrated Bioimaging, Berkeley, CA 94720 USA

[4] Univ Texas MD Anderson Canc Ctr, Dept Mol & Cellular Oncol, Houston, TX 77030 USA

来源：

NUCLEIC ACIDS RESEARCH | 2016年 / 44卷 / W1期

基金：

美国能源部; 美国国家卫生研究院;

关键词：

X-RAY-SCATTERING; DNA-REPAIR ENZYME; BIOLOGICAL MACROMOLECULES; COMPUTATION; RESOLUTION; DOCKING; CONFORMATIONS; SERVER;

D O I：

10.1093/nar/gkw389

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Small Angle X-ray Scattering (SAXS) is an increasingly common and useful technique for structural characterization of molecules in solution. A SAXS experiment determines the scattering intensity of a molecule as a function of spatial frequency, termed SAXS profile. Here, we describe three web servers for modeling atomic structures based on SAXS profiles. FoXS (Fast X-Ray Scattering) rapidly computes a SAXS profile of a given atomistic model and fits it to an experimental profile. FoXSDock docks two rigid protein structures based on a SAXS profile of their complex. MultiFoXS computes a population-weighted ensemble starting from a single input structure by fitting to a SAXS profile of the protein in solution. We describe the interfaces and capabilities of the servers (salilab.org/foxs), followed by demonstrating their application on Interleukin-33 (IL-33) and its primary receptor ST2.

引用

页码：W424 / W429

页数：6

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