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 [https://en.wikipedia.org/wiki/Molecular_diffusion 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.\<ref name="Robey">PMID:29643473</ref>. 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 have 2 transmembrane domains which work to recognize and transport the substrates across the [https://en.wikipedia.org/wiki/Cell_membrane plasma membrane] and out of the cell. The [https://en.wikipedia.org/wiki/Amino_acid residues] in the TMD provide the transporters each with specific substrates which they can transport. They also allow for the coupling of transport with [https://en.wikipedia.org/wiki/ATP_hydrolysis ATP hydrolysis] to transport molecules regardless of the [https://en.wikipedia.org/wiki/Molecular_diffusion 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 [https://en.wikipedia.org/wiki/Molecular_diffusion 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.<ref name="Robey">PMID:29643473</ref>. 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 have 2 transmembrane domains which work to recognize and transport the substrates across the [https://en.wikipedia.org/wiki/Cell_membrane plasma membrane] and out of the cell. The [https://en.wikipedia.org/wiki/Amino_acid residues] in the TMD provide the transporters each with specific substrates which they can transport. They also allow for the coupling of transport with [https://en.wikipedia.org/wiki/ATP_hydrolysis ATP hydrolysis] to transport molecules regardless of the [https://en.wikipedia.org/wiki/Molecular_diffusion concentration gradient].

===Specific Members of the Family===

As previously mentioned, 19 of the 48 members of the transporter family are involved in chemotherapeutic removal from the cell. Of these, three, <scene name='83/832939/Abcb1/1'>ABCB1</scene>, ABCG2 and <scene name='83/832939/Abcc1/1'>ABCC1</scene> were identified for further study and comparison of [https://en.wikipedia.org/wiki/Chemical_structure structure] due to their function as multi-drug transporters<ref name="Robey">PMID:29643473</ref>. The differences in their structures provided valuable information for scientific research into their substrate binding processes.

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 [https://en.wikipedia.org/wiki/Molecular_diffusion 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.\<ref name="Robey">PMID:29643473</ref>. 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 have 2 transmembrane domains which work to recognize and transport the substrates across the [https://en.wikipedia.org/wiki/Cell_membrane plasma membrane] and out of the cell. The [https://en.wikipedia.org/wiki/Amino_acid residues] in the TMD provide the transporters each with specific substrates which they can transport. They also allow for the coupling of transport with [https://en.wikipedia.org/wiki/ATP_hydrolysis ATP hydrolysis] to transport molecules regardless of the [https://en.wikipedia.org/wiki/Molecular_diffusion 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 [https://en.wikipedia.org/wiki/Molecular_diffusion 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.<ref name="Robey">PMID:29643473</ref>. 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 have 2 transmembrane domains which work to recognize and transport the substrates across the [https://en.wikipedia.org/wiki/Cell_membrane plasma membrane] and out of the cell. The [https://en.wikipedia.org/wiki/Amino_acid residues] in the TMD provide the transporters each with specific substrates which they can transport. They also allow for the coupling of transport with [https://en.wikipedia.org/wiki/ATP_hydrolysis ATP hydrolysis] to transport molecules regardless of the [https://en.wikipedia.org/wiki/Molecular_diffusion concentration gradient].
 ===Specific Members of the Family===
 As previously mentioned, 19 of the 48 members of the transporter family are involved in chemotherapeutic removal from the cell. Of these, three, <scene name='83/832939/Abcb1/1'>ABCB1</scene>, ABCG2 and <scene name='83/832939/Abcc1/1'>ABCC1</scene> were identified for further study and comparison of [https://en.wikipedia.org/wiki/Chemical_structure structure] due to their function as multi-drug transporters<ref name="Robey">PMID:29643473</ref>. The differences in their structures provided valuable information for scientific research into their substrate binding processes.