Back to Search Start Over

Template-free modeling by LEE and LEER in CASP11

Authors :
Qianyi Cheng
InSuk Joung
Sung Jong Lee
Jooyoung Lee
Jong Yun Kim
Sun Young Lee
Keehyoung Joo
Source :
Proteins: Structure, Function, and Bioinformatics. 84:118-130
Publication Year :
2015
Publisher :
Wiley, 2015.

Abstract

For the template-free modeling of human targets of CASP11, we utilized two of our modeling protocols, LEE and LEER. The LEE protocol took CASP11-released server models as the input and used some of them as templates for 3D (three-dimensional) modeling. The template selection procedure was based on the clustering of the server models aided by a community detection method of a server-model network. Restraining energy terms generated from the selected templates together with physical and statistical energy terms were used to build 3D models. Side-chains of the 3D models were rebuilt using target-specific consensus side-chain library along with the SCWRL4 rotamer library, which completed the LEE protocol. The first success factor of the LEE protocol was due to efficient server model screening. The average backbone accuracy of selected server models was similar to that of top 30% server models. The second factor was that a proper energy function along with our optimization method guided us, so that we successfully generated better quality models than the input template models. In 10 out of 24 cases, better backbone structures than the best of input template structures were generated. LEE models were further refined by performing restrained molecular dynamics simulations to generate LEER models. CASP11 results indicate that LEE models were better than the average template models in terms of both backbone structures and side-chain orientations. LEER models were of improved physical realism and stereo-chemistry compared to LEE models, and they were comparable to LEE models in the backbone accuracy. Proteins 2016; 84(Suppl 1):118-130. © 2015 Wiley Periodicals, Inc.

Details

ISSN :
08873585
Volume :
84
Database :
OpenAIRE
Journal :
Proteins: Structure, Function, and Bioinformatics
Accession number :
edsair.doi...........3076da9e7f3b6b747f6653a4281fc926