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 [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 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 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 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 structure due to their function as multi-drug transporters. The differences in their structures provided valuable information for scientific research into their substrate binding processes.

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. 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 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 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 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 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 structure due to their function as multi-drug transporters. The differences in their structures provided valuable information for scientific research into their substrate binding processes.
+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. The differences in their structures provided valuable information for scientific research into their substrate binding processes.