Sandbox Reserved 1613: Difference between revisions

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==ABC Transporter Family==

In the 1990's, [https://en.wikipedia.org/wiki/ATP-binding_cassette_transporter ABC binding cassette transporters] became the subject of much discussion as many were found to have links to the inhibition of anti-cancer therapies. All 48 members of the family were studied and several structural aspects were found to be important to the characterization of [https://en.wikipedia.org/wiki/Transport_protein transporters] in this family. The first was the presence of two [https://en.wikipedia.org/wiki/Nucleotide nucleotide] binding [https://en.wikipedia.org/wiki/Protein_domain domains] (NBD) located in the cytoplasm of all cells which bound and [https://en.wikipedia.org/wiki/Hydrolysis hydrolyzed] [https://en.wikipedia.org/wiki/Adenosine_triphosphate ATP], providing the necessary energy for transport of the substrate to occur. In all 7 subfamilies (A-G) of the ABC family, the NBD's are greatly conserved. Each transporter of this family is made unique by the structure and form of their specific transmembrane binding domain (TMD). Each of the 48 transporters also have 2 transmembrane domains which work to recognize and transport the substrates across the plasma membrane and out of the cell. The residues in the TMD provide the transporters each with specific substrates which they can transport. They also allow for the coupling of transport with ATP hydrolysis to transport molecules regardless of the concentration gradient.

In the 1990's, [https://en.wikipedia.org/wiki/ATP-binding_cassette_transporter ABC binding cassette transporters] became the subject of much discussion as many were found to have links to the inhibition of anti-cancer therapies. All 48 members of the family were studied and several structural aspects were found to be important to the characterization of [https://en.wikipedia.org/wiki/Transport_protein transporters] in this family. The first was the presence of two [https://en.wikipedia.org/wiki/Nucleotide nucleotide] binding [https://en.wikipedia.org/wiki/Protein_domain domains] (NBD) located in the cytoplasm of all cells which bound and [https://en.wikipedia.org/wiki/Hydrolysis hydrolyzed] [https://en.wikipedia.org/wiki/Adenosine_triphosphate ATP], providing the necessary energy for [https://en.wikipedia.org/wiki/Membrane_transport transport] of the [https://en.wikipedia.org/wiki/Substrate_(chemistry) substrate] to occur. In all 7 subfamilies (A-G) of the ABC family, the NBD's are greatly conserved. Each transporter of this family is made unique by the structure and form of their specific transmembrane binding domain (TMD). Each of the 48 transporters also have 2 transmembrane domains which work to recognize and transport the substrates across the plasma membrane and out of the cell. The residues in the TMD provide the transporters each with specific substrates which they can transport. They also allow for the coupling of transport with ATP hydrolysis to transport molecules regardless of the concentration gradient.

Sandbox Reserved 1613: Difference between revisions

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Revision as of 07:52, 21 April 2020 view source Samuel Sullivan (talk \| contribs) 70 edits No edit summary ← Older edit		Revision as of 07:54, 21 April 2020 view source Samuel Sullivan (talk \| contribs) 70 edits No edit summary Newer edit →
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	==ABC Transporter Family==		==ABC Transporter Family==
	In the 1990's, [https://en.wikipedia.org/wiki/ATP-binding_cassette_transporter ABC binding cassette transporters] became the subject of much discussion as many were found to have links to the inhibition of anti-cancer therapies. All 48 members of the family were studied and several structural aspects were found to be important to the characterization of [https://en.wikipedia.org/wiki/Transport_protein transporters] in this family. The first was the presence of two [https://en.wikipedia.org/wiki/Nucleotide nucleotide] binding [https://en.wikipedia.org/wiki/Protein_domain domains] (NBD) located in the cytoplasm of all cells which bound and [https://en.wikipedia.org/wiki/Hydrolysis hydrolyzed] [https://en.wikipedia.org/wiki/Adenosine_triphosphate ATP], providing the necessary energy for transport of the substrate to occur. In all 7 subfamilies (A-G) of the ABC family, the NBD's are greatly conserved. Each transporter of this family is made unique by the structure and form of their specific transmembrane binding domain (TMD). Each of the 48 transporters also have 2 transmembrane domains which work to recognize and transport the substrates across the plasma membrane and out of the cell. The residues in the TMD provide the transporters each with specific substrates which they can transport. They also allow for the coupling of transport with ATP hydrolysis to transport molecules regardless of the concentration gradient.		In the 1990's, [https://en.wikipedia.org/wiki/ATP-binding_cassette_transporter ABC binding cassette transporters] became the subject of much discussion as many were found to have links to the inhibition of anti-cancer therapies. All 48 members of the family were studied and several structural aspects were found to be important to the characterization of [https://en.wikipedia.org/wiki/Transport_protein transporters] in this family. The first was the presence of two [https://en.wikipedia.org/wiki/Nucleotide nucleotide] binding [https://en.wikipedia.org/wiki/Protein_domain domains] (NBD) located in the cytoplasm of all cells which bound and [https://en.wikipedia.org/wiki/Hydrolysis hydrolyzed] [https://en.wikipedia.org/wiki/Adenosine_triphosphate ATP], providing the necessary energy for [https://en.wikipedia.org/wiki/Membrane_transport transport] of the [https://en.wikipedia.org/wiki/Substrate_(chemistry) substrate] to occur. In all 7 subfamilies (A-G) of the ABC family, the NBD's are greatly conserved. Each transporter of this family is made unique by the structure and form of their specific transmembrane binding domain (TMD). Each of the 48 transporters also have 2 transmembrane domains which work to recognize and transport the substrates across the plasma membrane and out of the cell. The residues in the TMD provide the transporters each with specific substrates which they can transport. They also allow for the coupling of transport with ATP hydrolysis to transport molecules regardless of the concentration gradient.