Difference between revisions of "Part:BBa K3515010"
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Vitamin D Receptor Binding Protein (VDR) selectively binds vitamin D in its active site, inducing a conformation change in the N and C termini regions, respectively. This makes it a distinguishable candidate for in vivo or in vitro vitamin D monitoring using fluorescence resonance energy transfer (FRET). Coupling this protein with two fluorophores can permit vitamin D detection. Vitamin D detection is vital as vitamin D is used in cells for the regulation of phosphorus and calcium reabsorption, as well as stimulation/activation of proper immune system functioning. Vitamin D is also a crucial biomarker used in clinical medicine for tracking the progression and status of Chronic Kidney Disease (CKD) patients, patients with bone density problems, and patients with cardiovascular complications. As such a biosensor for vitamin D tracking may be of great interest to patients and clinicians. This part includes a mutated VDR to have a cysteine modification that will bind cysteine linker arms and be used for biosensor immobilization allowing the detection of vitamin D. | Vitamin D Receptor Binding Protein (VDR) selectively binds vitamin D in its active site, inducing a conformation change in the N and C termini regions, respectively. This makes it a distinguishable candidate for in vivo or in vitro vitamin D monitoring using fluorescence resonance energy transfer (FRET). Coupling this protein with two fluorophores can permit vitamin D detection. Vitamin D detection is vital as vitamin D is used in cells for the regulation of phosphorus and calcium reabsorption, as well as stimulation/activation of proper immune system functioning. Vitamin D is also a crucial biomarker used in clinical medicine for tracking the progression and status of Chronic Kidney Disease (CKD) patients, patients with bone density problems, and patients with cardiovascular complications. As such a biosensor for vitamin D tracking may be of great interest to patients and clinicians. This part includes a mutated VDR to have a cysteine modification that will bind cysteine linker arms and be used for biosensor immobilization allowing the detection of vitamin D. | ||
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| + | Cysteine immobilization modifications of binding protein. Protein structures were obtained from the RCSB Protein Data Bank. All protein residues are shown in a blue cartoon preset with cysteine residues labelled in red cartoon, respectively, using PyMOL software. | ||
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Latest revision as of 17:06, 29 May 2020
Vitamin D Receptor Binding Protein with cysteine modification(s) to bind to a biosensor.
Vitamin D Receptor Binding Protein (VDR) selectively binds vitamin D in its active site, inducing a conformation change in the N and C termini regions, respectively. This makes it a distinguishable candidate for in vivo or in vitro vitamin D monitoring using fluorescence resonance energy transfer (FRET). Coupling this protein with two fluorophores can permit vitamin D detection. Vitamin D detection is vital as vitamin D is used in cells for the regulation of phosphorus and calcium reabsorption, as well as stimulation/activation of proper immune system functioning. Vitamin D is also a crucial biomarker used in clinical medicine for tracking the progression and status of Chronic Kidney Disease (CKD) patients, patients with bone density problems, and patients with cardiovascular complications. As such a biosensor for vitamin D tracking may be of great interest to patients and clinicians. This part includes a mutated VDR to have a cysteine modification that will bind cysteine linker arms and be used for biosensor immobilization allowing the detection of vitamin D.
Cysteine immobilization modifications of binding protein. Protein structures were obtained from the RCSB Protein Data Bank. All protein residues are shown in a blue cartoon preset with cysteine residues labelled in red cartoon, respectively, using PyMOL software.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 189
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]