Sandbox GGC12 - Revision history

Student at 20:45, 28 April 2021

Student — Wed, 28 Apr 2021 20:45:37 GMT

←Older revision		Revision as of 20:45, 28 April 2021
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	The structural highlights of this protein are four: the three domains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.		The structural highlights of this protein are four: the three domains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.

-	This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. Digitoxin, cardiac glycoside, could bind domain I for cardiac insufficiency, warfarin, anticouagulant, bind primarily in domain II, and the diazapines like benzodiazapine, muscular relaxor, in domain III. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals. Sequence 143 through 155 and sequence 244 through 263 are involved in ligand binding. For example, residues <scene name='78/781196/Sequence/1'>143-155</scene>, an aromatic sequence,	+	This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. Digitoxin, cardiac glycoside, could bind domain I for cardiac insufficiency, warfarin, anticouagulant, bind primarily in domain II, and the diazapines like benzodiazapine, muscular relaxor, in domain III. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals. Sequence 143 through 155 and sequence 244 through 263 are involved in ligand binding. For example, residues <scene name='78/781196/Sequence/1'>143-155</scene>, an aromatic sequence, corresponds with the region of the second major long-chain fatty acid binding site <ref>PMID: 2155760</ref>.
-	corresponds with the region of the second major long-chain fatty acid binding site.	+

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Student at 20:39, 28 April 2021

Student — Wed, 28 Apr 2021 20:39:03 GMT

←Older revision		Revision as of 20:39, 28 April 2021
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	The structural highlights of this protein are four: the three domains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.		The structural highlights of this protein are four: the three domains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.

-	This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. ~~Warfarin~~, anticouagulant, ~~is believed to~~ bind primarily in domain II, and the diazapines like benzodiazapine, muscular relaxor, in	+	This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. Digitoxin, cardiac glycoside, could bind domain I for cardiac insufficiency, warfarin, anticouagulant, bind primarily in domain II, and the diazapines like benzodiazapine, muscular relaxor, in domain III. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals. Sequence 143 through 155 and sequence 244 through 263 are involved in ligand binding. For example, residues <scene name='78/781196/Sequence/1'>143-155</scene>, an aromatic sequence,
-	domain III. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals. Sequence 143 through 155 and sequence 244 through 263 are involved in ligand binding. For example, residues <scene name='78/781196/Sequence/1'>143-155</scene>, an aromatic sequence,	+
	corresponds with the region of the second major long-chain fatty acid binding site.		corresponds with the region of the second major long-chain fatty acid binding site.

Student at 19:57, 28 April 2021

Student — Wed, 28 Apr 2021 19:57:57 GMT

←Older revision		Revision as of 19:57, 28 April 2021
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	This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. Warfarin, anticouagulant, is believed to bind primarily in domain II, and the diazapines like benzodiazapine, muscular relaxor, in		This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. Warfarin, anticouagulant, is believed to bind primarily in domain II, and the diazapines like benzodiazapine, muscular relaxor, in
-	domain III. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals.	+	domain III. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals. Sequence 143 through 155 and sequence 244 through 263 are involved in ligand binding. For example, residues <scene name='78/781196/Sequence/1'>143-155</scene>, an aromatic sequence,
		+	corresponds with the region of the second major long-chain fatty acid binding site.

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Student at 19:50, 28 April 2021

Student — Wed, 28 Apr 2021 19:50:07 GMT

←Older revision		Revision as of 19:50, 28 April 2021
Line 19:		Line 19:
	The structural highlights of this protein are four: the three domains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.		The structural highlights of this protein are four: the three domains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.

-	This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals.	+	This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. Warfarin, anticouagulant, is believed to bind primarily in domain II, and the diazapines like benzodiazapine, muscular relaxor, in
		+	domain III. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals.

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Student at 19:12, 28 April 2021

Student — Wed, 28 Apr 2021 19:12:57 GMT

←Older revision		Revision as of 19:12, 28 April 2021
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	HSA is involved in two important diseases, Hyperthyroxinemia, familial dysalbuminemic (FDAH) and Analbuminemia (ANALBA).		HSA is involved in two important diseases, Hyperthyroxinemia, familial dysalbuminemic (FDAH) and Analbuminemia (ANALBA).

-	First, FDAH is a condition based on the genetic composition of the individual. It is caused by a mutation in the ALB gene, which corresponds to an increased affinity of the protein HSA for thyroxine. In detail, this autosomal dominant genetic disorder is characterized by the mutation of HSA causing the assembly of thyroxine in a higher proportion. There are two positions with three natural variants identified on the HSA that mutate to cause this disorder. The first position is at 90 amino acid, where leucine is replaced by a proline. The second position at 242 amino acid, where arginine is substituted by histidine or proline. This disorder could lead to confusion and several misdiagnoses of hyperthyroidism because it is difficult to detect it due to the normal TSH and free thyroxine levels but with an elevated total of thyroxine <ref>PMID: 32665066</ref>.	+	First, FDAH is a condition based on the genetic composition of the individual. It is caused by a mutation in the ALB gene, which corresponds to an increased affinity of the protein HSA for thyroxine. In detail, this autosomal dominant genetic disorder is characterized by the mutation of HSA causing the assembly of thyroxine in a higher proportion. There are two positions with three natural variants identified on the HSA that mutate to cause this disorder. The first position (red) is at 90 amino acid, where leucine is replaced by a proline. The second position (green) at 242 amino acid, where arginine is substituted by histidine or proline <scene name='78/781196/Hyperthyroxinemia/1'>3D View</scene>. This disorder could lead to confusion and several misdiagnoses of hyperthyroidism because it is difficult to detect it due to the normal TSH and free thyroxine levels but with an elevated total of thyroxine <ref>PMID: 32665066</ref>.

	Second, ANALBA is an uncommon autosomal recessive genetic mutation characterized by the identification of very low levels of HSA circulating in the bloodstream <ref>PMID: 8134387</ref>. The affected individuals have symptoms corresponding to mild edema, hypotension, fatigue, and lower body lipodystrophy in females. The mutagenesis is located in the position 91 where histidine is replaced by alanine impairing metal binding <ref>PMID: 28567254</ref>. The complications of this disorder could lead to early atherosclerosis and heart problems.		Second, ANALBA is an uncommon autosomal recessive genetic mutation characterized by the identification of very low levels of HSA circulating in the bloodstream <ref>PMID: 8134387</ref>. The affected individuals have symptoms corresponding to mild edema, hypotension, fatigue, and lower body lipodystrophy in females. The mutagenesis is located in the position 91 where histidine is replaced by alanine impairing metal binding <ref>PMID: 28567254</ref>. The complications of this disorder could lead to early atherosclerosis and heart problems.

Student at 18:56, 28 April 2021

Student — Wed, 28 Apr 2021 18:56:26 GMT

←Older revision		Revision as of 18:56, 28 April 2021
Line 17:		Line 17:

	== Structural highlights ==		== Structural highlights ==
-	The structural highlights of this protein are four: the ~~six subdomains~~ that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.	+	The structural highlights of this protein are four: the three domains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.

-	This is the structural view of <scene name='78/781196/~~Six_subdomains~~/1'>~~HSA six subdomains~~</scene> by different colors~~. nd another to make <scene name="/12/3456/Sample/2"> by different colors. a transparent representation</scene> of the protein~~. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals.	+	This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals.

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Student at 18:51, 28 April 2021

Student — Wed, 28 Apr 2021 18:51:07 GMT

←Older revision		Revision as of 18:51, 28 April 2021
Line 19:		Line 19:
	The structural highlights of this protein are four: the six subdomains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.		The structural highlights of this protein are four: the six subdomains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.

-	This is the structural view of <scene name='78/781196/Six_subdomains/1'>HSA six subdomains</scene> by different colors. nd another to make <scene name="/12/3456/Sample/2"> by different colors. a transparent representation</scene> of the protein. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes.	+	This is the structural view of <scene name='78/781196/Six_subdomains/1'>HSA six subdomains</scene> by different colors. nd another to make <scene name="/12/3456/Sample/2"> by different colors. a transparent representation</scene> of the protein. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals.

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Student at 18:38, 28 April 2021

Student — Wed, 28 Apr 2021 18:38:34 GMT

←Older revision		Revision as of 18:38, 28 April 2021
Line 19:		Line 19:
	The structural highlights of this protein are four: the six subdomains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.		The structural highlights of this protein are four: the six subdomains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.

-	This is the structural view of <scene name='78/781196/Six_subdomains/1'>HSA six subdomains</scene> by different colors. nd another to make <scene name="/12/3456/Sample/2"> by different colors. a transparent representation</scene> of the protein. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood.	+	This is the structural view of <scene name='78/781196/Six_subdomains/1'>HSA six subdomains</scene> by different colors. nd another to make <scene name="/12/3456/Sample/2"> by different colors. a transparent representation</scene> of the protein. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes.

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Student at 18:23, 28 April 2021

Student — Wed, 28 Apr 2021 18:23:47 GMT

←Older revision		Revision as of 18:23, 28 April 2021
Line 19:		Line 19:
	The structural highlights of this protein are four: the six subdomains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.		The structural highlights of this protein are four: the six subdomains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.

-	This is the structural view of <scene name='78/781196/Six_subdomains/1'>HSA six subdomains</scene> by different colors. nd another to make <scene name="/12/3456/Sample/2"> by different colors. a transparent representation</scene> of the protein. The shared binding site in domain II between zinc and calcium at residue Asp 273 suggests a crosstalk between zinc and calcium transport in the blood.	+	This is the structural view of <scene name='78/781196/Six_subdomains/1'>HSA six subdomains</scene> by different colors. nd another to make <scene name="/12/3456/Sample/2"> by different colors. a transparent representation</scene> of the protein. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood.

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Student at 18:14, 28 April 2021

Student — Wed, 28 Apr 2021 18:14:48 GMT

←Older revision		Revision as of 18:14, 28 April 2021
Line 19:		Line 19:
	The structural highlights of this protein are four: the six subdomains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.		The structural highlights of this protein are four: the six subdomains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>.

-	This is the structural view of <scene name='78/781196/Six_subdomains/1'>HSA six subdomains</scene> by different colors. nd another to make <scene name="/12/3456/Sample/2"> by different colors. a transparent representation</scene> of the protein. ~~You can make your own scenes on SAT starting from scratch or loading~~ and ~~editing one of these sample scenes~~.	+	This is the structural view of <scene name='78/781196/Six_subdomains/1'>HSA six subdomains</scene> by different colors. nd another to make <scene name="/12/3456/Sample/2"> by different colors. a transparent representation</scene> of the protein. The shared binding site in domain II between zinc and calcium at residue Asp 273 suggests a crosstalk between zinc and calcium transport in the blood.

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>