Triple resonance nuclear magnetic resonance backbone assignment of the ax I Domain integrin protein

dc.contributorŞen, Mehmet
dc.contributorFerreon, Josephine
dc.contributorAsmussen, Jennifer
dc.contributor.authorAbousaway, Omar
dc.date.accessioned2019-07-29T19:04:10Z
dc.date.available2019-07-29T19:04:10Z
dc.date.issued2019-05
dc.description.abstractThe I-domain of the ax integrin subunit binds extracellular ligands, such as iC3b, a complement factor in the innate immune system. The expression of the axb2 integrin on immune cells, such as dendritic cells, macrophages, and monocytes, suggests an in important role in the immune system. Integrin proteins are able to bind ligands when in the "open" conformation, but not and if so with limited affinity in the "closed" conformation. NMR experiments are able to probe molecular motions at the nanosecond timescale, and are thus ideal for studying the transition between the open and closed states in integrins. Here, we report the triple resonance NMR backbone assignment of the ax I-domain integrin, as a preliminary experiment for future structural and dynamic studies.
dc.description.departmentBiology and Biochemistry, Department of
dc.description.departmentHonors College
dc.identifier.citationPortions of this document appear in: Manandhar, P., Abousaway, O., Le, T., and Sen, M. (2017). Role of structural dynamics in leukocyte integrins function : interplay between the shape-shifting mechanism and allostery. International Journal of Cell Science and Molecular Biology 3, 1–4.en
dc.identifier.citationPortions of this document appear in: Manandhar, P., Abousaway, O., Le, T., and Sen, M. (2017). Role of structural dynamics in leukocyte integrins function : interplay between the shape-shifting mechanism and allostery. International Journal of Cell Science and Molecular Biology 3, 1–4.
dc.identifier.urihttps://hdl.handle.net/10657/4254
dc.language.isoen
dc.relation.ispartofSenior Honors Theses
dc.rightsThe author of this work is the copyright owner. UH Libraries and the Texas Digital Library have their permission to store and provide access to this work. UH Libraries has secured permission to reproduce any and all previously published materials contained in the work. Further transmission, reproduction, or presentation of this work is prohibited except with permission of the author(s).
dc.titleTriple resonance nuclear magnetic resonance backbone assignment of the ax I Domain integrin protein
dc.typeHonors Thesis
dc.type.dcmiText
thesis.degree.collegeCollege of Natural Sciences and Mathematics
thesis.degree.levelBachelors
thesis.degree.nameBachelor of Science

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