Sentences with phrase «cytoplasmic tail»
The term "cytoplasmic tail" refers to a part of a protein that is located inside a cell. It is like a "tail" that extends into the cytoplasm, the jelly-like substance within a cell. This tail is important for the function and signaling of the protein, as it interacts with other molecules within the cell to carry out its tasks. Full definition
When the Saad group put molecules of the intact, full - length cytoplasmic tail of gp41 into the micelle solution, they found that the structures of each of the pieces were maintained in the intact structure.
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4 - 1BB (CD137) is a 30 kD type I glycoprotein and again a typical transmembrane receptor in the TNFR superfamily, containing 4 full cysteine rich domains, and a relatively short cytoplasmic tail, and also signals as a trimer when bound to 4 - 1BBL, its known ligand in the TNF family.
Saad says knowledge of the gp41 cytoplasmic tail structure will also open comparative studies of 10 different retroviruses that have similar tails to learn why some tails are shorter and some tails are longer.
One gene known to be important in maintaining apical - basal polarity and assisting in the formation of adherens junctions in the retina is Crumbs (Crb), which encodes a transmembrane protein containing a long extracellular domain and a short C - terminal cytoplasmic tail.
OX40 (CD134) is a 50 kD type I transmembrane glycoprotein in the TNFR superfamily, containing 3 full cysteine rich domains, and a relatively short cytoplasmic tail, and although a monomer it signals as a trimer when bound to OX40L, its known ligand in the TNF family.
Even then, 70 percent of the cytoplasmic tail was cut and only 30 percent was left intact.
Cytoplasmic tail of gp41 The structures of three membrane - associated cytoplasmic tails of gp41 are shown in red and orange, from this illustration of the trimeric spike structure.
«The cytoplasmic tail of gp41 has been of interest for a long time, and nobody understands how it functions in infection or how it helps incorporate the envelope protein into the membrane,» Saad said.
The structure of the cytoplasmic tail of gp41 was a tremendously difficult task to solve, says Saad, an associate professor of microbiology at UAB.
The UAB group also showed the preferred topology of the cytoplasmic tail when bound to the membrane.
The cytoplasmic tail appears to play a key role in virus assembly to help incorporate the envelope spike structures into the surface of viral particles.
The cytoplasmic tail is a critical component of infectivity.»
Knowledge of this structure, called the cytoplasmic tail of gp41 protein, will help researchers further understand how the virus infects human cells and how progeny viruses are assembled and released from infected cells.
They found that the N - terminal end of the cytoplasmic tail of gp41, measuring 45 amino acid residues, lacked a regular secondary structure and was not associated with the membrane, which wraps around an HIV - 1 viral particle like the leather cover of a baseball.
Saad says the structure opens up whole new areas of research: How the cytoplasmic tail stabilizes the envelope protein structure, how it affects membrane mobility of the envelope protein structure, and how it helps coordinate membrane - binding and the association of 2,000 HIV - 1 Gag polyproteins underneath the membrane surface.
One problem for Saad and his UAB colleagues came as they tried to express the cytoplasmic tail of gp41 in growing E. coli cells.
The C - terminal end of the cytoplasmic tail of gp41, measuring 105 amino acid residues, was tightly associated to the membrane and had three alpha - helixes with portions that were hydrophobic and portions that were hydrophilic.
As full length Bk132 Env would not pseudotype on an NL43 HIV core we truncated the cytoplasmic tail of the Envs [49], [50], and conducted tropism testing on NP2 cell lines expressing CD4 with either CCR5 or CXCR4.