5x52 - Revision history

OCA at 07:54, 22 November 2023

OCA — Wed, 22 Nov 2023 07:54:04 GMT

←Older revision		Revision as of 07:54, 22 November 2023
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	<StructureSection load='5x52' size='340' side='right'caption='[[5x52]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='5x52' size='340' side='right'caption='[[5x52]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5x52]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X52 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5X52 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5x52]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X52 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AME:N-ACETYLMETHIONINE'>AME</scene>, <scene name='pdbligand=OCA:OCTANOIC+ACID+(CAPRYLIC+ACID)'>OCA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 3.005Å</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x52 OCA], [~~http~~://pdbe.org/5x52 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5x52 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5x52 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5x52 ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AME:N-ACETYLMETHIONINE'>AME</scene>, <scene name='pdbligand=OCA:OCTANOIC+ACID+(CAPRYLIC+ACID)'>OCA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x52 OCA], [https://pdbe.org/5x52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x52 RCSB], [https://www.ebi.ac.uk/pdbsum/5x52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x52 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN]] Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:[~~http~~://omim.org/entry/103600 103600]]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.<ref>PMID:8048949</ref> <ref>PMID:7852505</ref> <ref>PMID:9329347</ref> <ref>PMID:9589637</ref>	+	[https://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN] Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:[https://omim.org/entry/103600 103600]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.<ref>PMID:8048949</ref> <ref>PMID:7852505</ref> <ref>PMID:9329347</ref> <ref>PMID:9589637</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN]] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.<ref>PMID:19021548</ref>	+	[https://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.<ref>PMID:19021548</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Kawai, A]]	+	[[Category: Kawai A]]
-	[[Category: Otagiri, M]]	+	[[Category: Otagiri M]]
-	~~[[Category: Transport protein~~]]	+

OCA at 07:25, 7 October 2020

OCA — Wed, 07 Oct 2020 07:25:38 GMT

←Older revision		Revision as of 07:25, 7 October 2020
Line 1:		Line 1:

	==Human serum albumin complexed with octanoate and N-acetyl-L-methionine==		==Human serum albumin complexed with octanoate and N-acetyl-L-methionine==
-	<StructureSection load='5x52' size='340' side='right' caption='[[5x52]], [[Resolution\|resolution]] 3.00Å' scene=''>	+	<StructureSection load='5x52' size='340' side='right'caption='[[5x52]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5x52]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X52 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5X52 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5x52]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X52 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X52 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AME:N-ACETYLMETHIONINE'>AME</scene>, <scene name='pdbligand=OCA:OCTANOIC+ACID+(CAPRYLIC+ACID)'>OCA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AME:N-ACETYLMETHIONINE'>AME</scene>, <scene name='pdbligand=OCA:OCTANOIC+ACID+(CAPRYLIC+ACID)'>OCA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x52 OCA], [http://pdbe.org/5x52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x52 RCSB], [http://www.ebi.ac.uk/pdbsum/5x52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x52 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x52 OCA], [http://pdbe.org/5x52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x52 RCSB], [http://www.ebi.ac.uk/pdbsum/5x52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x52 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	</div>		</div>
	<div class="pdbe-citations 5x52" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5x52" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Albumin 3D structures\|Albumin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Kawai, A]]		[[Category: Kawai, A]]
	[[Category: Otagiri, M]]		[[Category: Otagiri, M]]
	[[Category: Transport protein]]		[[Category: Transport protein]]

OCA at 15:43, 17 May 2017

OCA — Wed, 17 May 2017 15:43:04 GMT

←Older revision		Revision as of 15:43, 17 May 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5x52 is ~~ON HOLD~~	+	==Human serum albumin complexed with octanoate and N-acetyl-L-methionine==
		+	<StructureSection load='5x52' size='340' side='right' caption='[[5x52]], [[Resolution\|resolution]] 3.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5x52]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X52 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AME:N-ACETYLMETHIONINE'>AME</scene>, <scene name='pdbligand=OCA:OCTANOIC+ACID+(CAPRYLIC+ACID)'>OCA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5x52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x52 OCA], [http://pdbe.org/5x52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x52 RCSB], [http://www.ebi.ac.uk/pdbsum/5x52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x52 ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN]] Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:[http://omim.org/entry/103600 103600]]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.<ref>PMID:8048949</ref> <ref>PMID:7852505</ref> <ref>PMID:9329347</ref> <ref>PMID:9589637</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN]] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.<ref>PMID:19021548</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	During pasteurization and storage of albumin products, Sodium octanoate (Oct) and N-acethyl-L-tryptophan (N-AcTrp) are used as the thermal stabilizer and the antioxidant for human serum albumin (HSA), respectively. We recently reported that N-acethyl-L-methionine (N-AcMet) is an antioxidant for HSA, which is superior to N-AcTrp when it is especially exposed to light during storage. The objective of the present study is to clarify the molecular mechanism responsible for the HSA protective effect of Oct and N-AcMet based on their ternary complex structure. Crystal structure of the HSA-Oct-N-AcMet complex showed that one N-AcMet molecule is bound to the entrance of drug site 1 of HSA, and its side chain, which is susceptible to the oxidation, is exposed to the solvent. At the same time, two Oct binding sites are observed in drug sites 1 and 2 of HSA, respectively, and each Oct molecule occupies the hydrophobic cavity in them. These results indicate the molecular mechanism responsible for the HSA stabilization by these small molecules as follows. N-AcMet seals the entrance of drug site 1 while it acts as an antioxidant for HSA. Oct is chiefly bound to drug site 2 of HSA and it increases the thermal stability of HSA because of the occupying the largest intra-cavity of sub-domain IIIA in HSA. These findings suggest that N-AcMet acts positively as useful stabilizer for albumin formulated products such as functionalized HSA and HSA fusion proteins.

-	~~Authors~~:	+	Crystallographic analysis of the Ternary Complex of Octanoate and N-acetyl-L-methionine with Human Serum Albumin Reveals the Mode of their Stabilizing Interactions.,Kawai A, Chuang VTG, Kouno Y, Yamasaki K, Miyamoto S, Anraku M, Otagiri M Biochim Biophys Acta. 2017 May 1. pii: S1570-9639(17)30080-8. doi:, 10.1016/j.bbapap.2017.04.004. PMID:28473296<ref>PMID:28473296</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5x52" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Kawai, A]]
		+	[[Category: Otagiri, M]]
		+	[[Category: Transport protein]]

OCA: Protected "5x52" [edit=sysop:move=sysop]

OCA — Thu, 09 Mar 2017 15:45:39 GMT

Protected "5x52" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:45, 9 March 2017

OCA: New page: '''Unreleased structure''' The entry 5x52 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Thu, 09 Mar 2017 15:45:38 GMT

New page: '''Unreleased structure''' The entry 5x52 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5x52 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]