CampbellUniversity (Buies Creek NC)
Complex of Ran with Importin Beta
Team members: Najla Kawas, Juli Osborne, Prathna Raval and Travis Rhea
Faculty advisor: Karen Guzman, Ph.D.
Research Mentor: Greg Buhrman, Ph.D., North Carolina State University
PDB ID: 1ibr
Abstract
We wanted to highlight the areas of the complex that interact with the Nuclear Pore Complex (NPC) as it travels through the NPC for nuclear export, as well as the areas that change after Importin Beta and Ran GTP separate.
Campbell University (Buies Creek NC)
Importin Beta Complexed with IBB Domain of Importin Alpha
Team members: Emily Linton, Cameron Howell, Miranda Griffin and Julianne Nance
Faculty advisor: Karen Guzman, Ph.D.
Research Mentor: Greg Buhrman, Ph.D., North Carolina State University
PDB ID: 1qgk
Abstract
This model contains the human importin beta complexed with the IBB domain of Importin alpha. IBB stands for “Importin Beta Binding” and is an important domain in nuclear transport (Lott & Cingolani, 2011). The model is designed to show the sidechains involved in the interaction between importin beta and the IBB domain of importin alpha.
Campbell University (Buies Creek NC)
Cse1p:Kap60p:RanGTP complex
Team members: Sharidan Hill, Sarah Ryals and Nehemiah Allen
Faculty advisor: Karen Guzman, Ph.D.
Research Mentor: Greg Buhrman, Ph.D., North Carolina State University
PDB ID: 1wa5
Abstract
This model is designed to represent the interactions between the different proteins and how they fit together in this export complex.
Saint Leo University (Saint Leo FL)
Hemagglutinin HA (H1, H2, H3, and H5)
Team member: Olivia Uribe
Faculty advisor: Audrey Shor, Ph.D.
PDB IDs: 3HTO, 2WR2, 1MQN, 1JSM
Abstract
Influenza A has been the cause of numerous deaths worldwide and is a virus that is constantly evolving. This virus is one that is seasonal and common in humans, however, avian species are particularly affected, especially water-fowl which are the natural hosts of this virus.
The influenza A viruses are classified based upon the antigenic properties of 17 hemagglutinin and 10 neuraminidase subtypes. Hemagglutinin, a surface glycoprotein, plays a critical role in host recognition, attachment, and entry. The protein is a homo-trimer, with each monomer comprised of two subunits (HA1 and HA2). HA1 contains a globular head that forms the sialic acid receptor binding site and stems from the base of the structure. The globular region of the protein is highly exposed and a major target of antibody recognition. The HA2 peptide is responsible for facilitating viral entry and endosomal membrane fusion.
This study investigates the invariable and highly variable regions of hemagglutinin H1, H2, H3, and H5 avian influenza subtypes. The areas of secondary structural conservation were identified and highlighted on the models. The sidechains of amino acids that differ significantly between the four subtypes are displayed on the models.
Saint Leo University (SaintLeo FL)
Discovering the Molecular Mechamism of STX1A in Asperger Syndrome
Team member: Carl Shotwell
Faculty advisor: Cheryl Clauson, Ph.D.
Theoretical Structure: Syntaxin 1A (stx1a)
Abstract
Syntaxin-1A is a member of the syntaxin superfamily. These types of proteins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane. Stx1a has an N-terminal regulatory and single C- terminal transmembrane domain that is also a SNARE domain (known as H3). Syntaxins bind synaptotagmin in a calcium-dependent fashion and interact with voltage dependent calcium and potassium channels via the C-terminal H3 domain. Syntaxin-1A is a key protein in ion channel regulation and synaptic exocytosis. Stx1a is associated with Williams-Beuren Syndrome (WBS) and has been implicated to be involved with Asperger Syndrome. WBS is a rare neurological disorder that is characterized by unusual facial features, cardiovascular defects, hypercalcemia, development delay followed by strong verbal skills, and an unusual ease with strangers. Asperger Syndrome also has a preservation of linguistic development but it is coupled with impairments in social interaction and nonverbal communication as well as restricted and repetitive patterns of behaviors and interests. However, the molecular mechanism of the protein has yet to be determined. Thus, this study investigates the impact of several SNPs that cause missense mutations on stx1a binding capacity.