Exploring Human Diseases and Biological Mechanisms by Protein Structure Prediction and Modeling.
Protein structure prediction and modeling provide a tool for understanding protein functions by computationally constructing protein structures from amino acid sequences and analyzing them. With help from protein prediction tools and web servers, users can obtain the three-dimensional protein structure models and gain knowledge of functions from the proteins. In this chapter, we will provide several examples of such studies. As an example, structure modeling methods were used to investigate the relation between mutation-caused misfolding of protein and human diseases including epilepsy and leukemia. Protein structure prediction and modeling were also applied in nucleotide-gated channels and their interaction interfaces to investigate their roles in brain and heart cells. In molecular mechanism studies of plants, rice salinity tolerance mechanism was studied via structure modeling on crucial proteins identified by systems biology analysis; trait-associated protein-protein interactions were modeled, which sheds some light on the roles of mutations in soybean oil/protein content. In the age of precision medicine, we believe protein structure prediction and modeling will play more and more important roles in investigating biomedical mechanism of diseases and drug design.
Department of Computer Science, University of Missouri, Columbia, MO, 65211, USA.|Christopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO, 65211, USA.
Juexin
J
Wang
School of Computing, University of Southern Mississippi, 118 College Drive, Hattiesburg, MS, 39406, USA.
Joseph
J
Luttrell
Christopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO, 65211, USA.|Informatics Institute, University of Missouri, Columbia, MO, 65211, USA.
Ning
N
Zhang
Christopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO, 65211, USA.|Informatics Institute, University of Missouri, Columbia, MO, 65211, USA.
Saad
S
Khan
Department of Medicine, Division of Cardiovascular Medicine, University of Wisconsin, Room 8418, 1111 Highland Ave, Madison, WI, 53706, USA.
NianQing
N
Shi
Department of Pathology and Anatomical Sciences, University of Missouri, Columbia, MO, 65211, USA.
Michael X
MX
Wang
Department of Neurology, Vanderbilt University Medical Center, Nashville, TN, 37232, USA.
Jing-Qiong
JQ
Kang
School of Computing, University of Southern Mississippi, 118 College Drive, Hattiesburg, MS, 39406, USA.
Zheng
Z
Wang
Department of Computer Science, University of Missouri, Columbia, MO, 65211, USA. xudong@missouri.edu.|Christopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO, 65211, USA. xudong@missouri.edu.|Informatics Institute, University of Missouri, Columbia, MO, 65211, USA. xudong@missouri.edu.
Dong
D
Xu
D000595:Amino Acid Sequence; D001921:Brain / Q000378:metabolism* / Q000473:pathology; D053453:Caspase 9 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D051244:Caveolin 3 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019295:Computational Biology / Q000379:methods*; D004827:Epilepsy / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D055106:Genome-Wide Association Study; D006801:Humans; D064428:Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008024:Ligands; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D012275:Oryza / Q000235:genetics; D000069600:Plant Breeding; D015221:Potassium Channels / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D057285:Precision Medicine / Q000379:methods*; D011485:Protein Binding; D011487:Protein Conformation; D011963:Receptors, GABA-A / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D012984:Software
C417736:CAV3 protein, human; D051244:Caveolin 3; C546279:GABRG2 protein, human; C578710:HCN2 protein, human; D064428:Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels; D008024:Ligands; D015221:Potassium Channels; D011963:Receptors, GABA-A; C506433:CASP9 protein, human; D053453:Caspase 9
Biological mechanism; GWAS; Human disease; Plant breeding; Protein misfolding; Protein structure modeling; Protein structure prediction; Sequence mutation