Next Article in Journal
Claudin 4 Is Differentially Expressed between Ovarian Cancer Subtypes and Plays a Role in Spheroid Formation
Next Article in Special Issue
Anchoring Intrinsically Disordered Proteins to Multiple Targets: Lessons from N-Terminus of the p53 Protein
Previous Article in Journal
The Effects of G-CSF on Proliferation of Mouse Myocardial Microvascular Endothelial Cells
Previous Article in Special Issue
The Role of Reactive-Oxygen-Species in Microbial Persistence and Inflammation
Article Menu

Export Article

Open AccessReview
Int. J. Mol. Sci. 2011, 12(2), 1316-1333;

Accounting for Large Amplitude Protein Deformation during in Silico Macromolecular Docking

LABIS, Genoscope, CEA, 2 rue Gaston Cremieux, F-91057 Evry Cedex, France
MTI, INSERM UMR-S 973, Paris Diderot-Paris 7 University, Bât Lamarck, 35 rue Hélène Brion, F-75205 Paris Cedex 13, France
LBT-UPR 9080 CNRS, IBPC, 13 rue Pierre et Marie Curie, F-75005 Paris, France
Author to whom correspondence should be addressed.
Received: 10 December 2010 / Revised: 7 January 2011 / Accepted: 8 February 2011 / Published: 22 February 2011
(This article belongs to the Special Issue Advances in Molecular Recognition)
Full-Text   |   PDF [1538 KB, uploaded 19 June 2014]   |  


Rapid progress of theoretical methods and computer calculation resources has turned in silico methods into a conceivable tool to predict the 3D structure of macromolecular assemblages, starting from the structure of their separate elements. Still, some classes of complexes represent a real challenge for macromolecular docking methods. In these complexes, protein parts like loops or domains undergo large amplitude deformations upon association, thus remodeling the surface accessible to the partner protein or DNA.We discuss the problems linked with managing such rearrangements in docking methods and we review strategies that are presently being explored, as well as their limitations and success. View Full-Text
Keywords: macromolecular docking; flexibility; protein loops and domains macromolecular docking; flexibility; protein loops and domains

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Share & Cite This Article

MDPI and ACS Style

Bastard, K.; Saladin, A.; Prévost, C. Accounting for Large Amplitude Protein Deformation during in Silico Macromolecular Docking. Int. J. Mol. Sci. 2011, 12, 1316-1333.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top