Part:BBa_K4990012
Tumor-Targeting Rod
Usage in short
You can use it to achieve BL-CRC adhesion.
You need to know
Acurate targeting is one important characteristics for many emerging cancer therapies, that is also what ourproject’s ambition. We designed two fusion proteins, they function like fishingrod, so we gave them the name: Fishing Rod Proteins (FRPs). The one that targetFn names Bacteria Tageting Rod(BTR), the other that target CRC cells names Tumor Tageting Rod(TTR). FRPs are displayed on engineered BL membranes, helping BLtarget to the correct place. Of course, their targets are cancer cells and Fn,rather than fish. Each FRP consists of four parts (Figure1): the signal peptide(white),helping FRPs locate on cell membrane; the membrane protein(pink), the base ofFRPs; and the linker(blue), helping FRPs become flexible; and the targeting fragments(yellow), the most pivotal role in FRPs
What is it
It consists of the GL-BP membrane protein, three repeated G4S linker peptides, and HlpA. Essentially, it involves the surface display technique to express HlpA on the BL membrane for adhesion to HSPG, thereby achieving adhesion between BL and CRC.
How it works
The HlpA monomer has been used in designing fusion proteins, as it can bind to HSPG on the surface of colorectal cancer cells. Hence, if you wish to target colorectal cancer cells with a protein, you can design a fusion protein attaching HlpA to one end. If you aim to make a cell target colorectal cancer cells, you can custom design a membrane protein containing HlpA for your chassis cell. Through surface display technology, expressing HlpA on the chassis cell surface would allow it to target colorectal cancer cells [2-4].
Examination of the DNA-binding region of Hlp revealed that this area is primarily composed of positively charged residues that form a pocket to accommodate DNA binding. The specific residues that comprise the DNA-binding pocket are depicted in Figure below. It should be noted that the side-chain electron density for Arg56, Lys60, Lys71 and Lys73 of subunit A and Arg54, Lys76 and Lys81 of subunit B was partially disordered and could not be traced in the electrondensity maps. Therefore, the side chains were modeled in idealized rotamer positions for the electrostatic surface calculations.[1]
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 358
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 358
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 771
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 358
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 358
Illegal NgoMIV site found at 1050
Illegal NgoMIV site found at 1590 - 1000COMPATIBLE WITH RFC[1000]
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