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C-terminus and P2X purinoreceptor

Shortcuts: Differences, Similarities, Jaccard Similarity Coefficient, References.

Difference between C-terminus and P2X purinoreceptor

C-terminus vs. P2X purinoreceptor

The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). The ATP-gated P2X receptor cation channel family, or simply P2X receptor family, consists of cation-permeable ligand-gated ion channels that open in response to the binding of extracellular adenosine 5'-triphosphate (ATP).

Similarities between C-terminus and P2X purinoreceptor

C-terminus and P2X purinoreceptor have 3 things in common (in Unionpedia): Endoplasmic reticulum, N-terminus, Transmembrane domain.

Endoplasmic reticulum

The endoplasmic reticulum (ER) is a type of organelle found in eukaryotic cells that forms an interconnected network of flattened, membrane-enclosed sacs or tube-like structures known as cisternae.

C-terminus and Endoplasmic reticulum · Endoplasmic reticulum and P2X purinoreceptor · See more »

N-terminus

The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide referring to the free amine group (-NH2) located at the end of a polypeptide.

C-terminus and N-terminus · N-terminus and P2X purinoreceptor · See more »

Transmembrane domain

Transmembrane domain usually denotes a transmembrane segment of single alpha helix of a transmembrane protein.

C-terminus and Transmembrane domain · P2X purinoreceptor and Transmembrane domain · See more »

The list above answers the following questions

C-terminus and P2X purinoreceptor Comparison

C-terminus has 30 relations, while P2X purinoreceptor has 78. As they have in common 3, the Jaccard index is 2.78% = 3 / (30 + 78).

References

This article shows the relationship between C-terminus and P2X purinoreceptor. To access each article from which the information was extracted, please visit:

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