Unknown

Dataset Information

0

Multidomain Assembler (MDA) Generates Models of Large Multidomain Proteins.


ABSTRACT: Homology modeling predicts protein structures using known structures of related proteins as templates. We developed MULTIDOMAIN ASSEMBLER (MDA) to address the special problems that arise when modeling proteins with large numbers of domains, such as fibronectin with 30 domains, as well as cases with hundreds of templates. These problems include how to spatially arrange nonoverlapping template structures, and how to get the best template coverage when some sequence regions have hundreds of available structures while other regions have a few distant homologs. MDA automates the tasks of template searching, visualization, and selection followed by multidomain model generation, and is part of the widely used molecular graphics package UCSF CHIMERA (University of California, San Francisco). We demonstrate applications and discuss MDA's benefits and limitations.

SUBMITTER: Hertig S 

PROVIDER: S-EPMC4423039 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Multidomain Assembler (MDA) Generates Models of Large Multidomain Proteins.

Hertig Samuel S   Goddard Thomas D TD   Johnson Graham T GT   Ferrin Thomas E TE  

Biophysical journal 20150501 9


Homology modeling predicts protein structures using known structures of related proteins as templates. We developed MULTIDOMAIN ASSEMBLER (MDA) to address the special problems that arise when modeling proteins with large numbers of domains, such as fibronectin with 30 domains, as well as cases with hundreds of templates. These problems include how to spatially arrange nonoverlapping template structures, and how to get the best template coverage when some sequence regions have hundreds of availab  ...[more]

Similar Datasets

| S-EPMC3535605 | biostudies-literature
| S-EPMC5533105 | biostudies-literature
| S-EPMC3767511 | biostudies-literature
| S-EPMC2645590 | biostudies-literature
| S-EPMC8479633 | biostudies-literature
| S-EPMC4862688 | biostudies-literature
| S-EPMC7611342 | biostudies-literature
| S-EPMC3855066 | biostudies-literature
| S-EPMC1815482 | biostudies-literature
| S-EPMC2544545 | biostudies-literature