8a2m - Revision history

OCA at 08:08, 7 February 2024

2024-02-07T08:08:28Z

← Older revision		Revision as of 08:08, 7 February 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8a2m]] is a 1 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=8A2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A2M FirstGlance]. <br>		<table><tr><td colspan='2'>[[8a2m]] is a 1 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=8A2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A2M FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.57Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8a2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a2m OCA], [https://pdbe.org/8a2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a2m RCSB], [https://www.ebi.ac.uk/pdbsum/8a2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a2m ProSAT]</span></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=8a2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a2m OCA], [https://pdbe.org/8a2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a2m RCSB], [https://www.ebi.ac.uk/pdbsum/8a2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a2m ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).		[https://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	For their easy and high-yield recombinant production, their high stability in a wide range of physico-chemical conditions and their characteristic hollow structure, ferritins (Fts) are considered useful scaffolds to encapsulate bioactive molecules. Notably, for the absence of immunogenicity and the selective interaction with tumor cells, the nanocages constituted by the heavy chain of the human variant of ferritin (hHFt) are optimal candidates for the delivery of anti-cancer drugs. hHFt nanocages can be disassembled and reassembled in vitro to allow the loading of cargo molecules, however the currently available protocols present some relevant drawbacks. Indeed, protein disassembly is achieved by exposure to extreme pH (either acidic or alkaline), followed by incubation at neutral pH to allow reassembly, but the final protein recovery and homogeneity are not satisfactory. Moreover, the exposure to extreme pH may affect the structure of the molecule to be loaded. In this paper, we report an alternative, efficient and reproducible procedure to reversibly disassemble hHFt under mild pH conditions. We demonstrate that a small amount of sodium dodecyl sulfate (SDS) is sufficient to disassemble the nanocage, which quantitatively reassembles upon SDS removal. Electron microscopy and X-ray crystallography show that the reassembled protein is identical to the untreated one. The newly developed procedure was used to encapsulate two small molecules. When compared to the existing disassembly/reassembly procedures, our approach can be applied in a wide range of pH values and temperatures, is compatible with a larger number of cargos and allows a higher protein recovery.

	A new and efficient procedure to load bioactive molecules within the human heavy-chain ferritin nanocage.,Lucignano R, Stanzione I, Ferraro G, Di Girolamo R, Cane C, Di Somma A, Duilio A, Merlino A, Picone D Front Mol Biosci. 2023 Jan 13;10:1008985. doi: 10.3389/fmolb.2023.1008985. , eCollection 2023. PMID:36714262<ref>PMID:36714262</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 8a2m" style="background-color:#fffaf0;"></div>~~
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:45, 8 February 2023

2023-02-08T06:45:05Z

← Older revision		Revision as of 06:45, 8 February 2023
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	~~'''Unreleased structure'''~~

	~~The entry~~ 8a2m is ~~ON HOLD until Paper~~ Publication		==X-ray structure of Ru(bpy)3]2+ complex (Ru1)-encapsulated human heavy chain ferritin==
			<StructureSection load='8a2m' size='340' side='right'caption='[[8a2m]], [[Resolution\|resolution]] 1.57Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[8a2m]] is a 1 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=8A2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A2M FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8a2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a2m OCA], [https://pdbe.org/8a2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a2m RCSB], [https://www.ebi.ac.uk/pdbsum/8a2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a2m ProSAT]</span></td></tr>
			</table>
			== Function ==
			[https://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			For their easy and high-yield recombinant production, their high stability in a wide range of physico-chemical conditions and their characteristic hollow structure, ferritins (Fts) are considered useful scaffolds to encapsulate bioactive molecules. Notably, for the absence of immunogenicity and the selective interaction with tumor cells, the nanocages constituted by the heavy chain of the human variant of ferritin (hHFt) are optimal candidates for the delivery of anti-cancer drugs. hHFt nanocages can be disassembled and reassembled in vitro to allow the loading of cargo molecules, however the currently available protocols present some relevant drawbacks. Indeed, protein disassembly is achieved by exposure to extreme pH (either acidic or alkaline), followed by incubation at neutral pH to allow reassembly, but the final protein recovery and homogeneity are not satisfactory. Moreover, the exposure to extreme pH may affect the structure of the molecule to be loaded. In this paper, we report an alternative, efficient and reproducible procedure to reversibly disassemble hHFt under mild pH conditions. We demonstrate that a small amount of sodium dodecyl sulfate (SDS) is sufficient to disassemble the nanocage, which quantitatively reassembles upon SDS removal. Electron microscopy and X-ray crystallography show that the reassembled protein is identical to the untreated one. The newly developed procedure was used to encapsulate two small molecules. When compared to the existing disassembly/reassembly procedures, our approach can be applied in a wide range of pH values and temperatures, is compatible with a larger number of cargos and allows a higher protein recovery.

	~~Authors:~~ Ferraro, G., Merlino, A.		A new and efficient procedure to load bioactive molecules within the human heavy-chain ferritin nanocage.,Lucignano R, Stanzione I, Ferraro G, Di Girolamo R, Cane C, Di Somma A, Duilio A, Merlino A, Picone D Front Mol Biosci. 2023 Jan 13;10:1008985. doi: 10.3389/fmolb.2023.1008985. , eCollection 2023. PMID:36714262<ref>PMID:36714262</ref>

	~~Description~~: ~~X-ray structure of Ru(bpy)3~~]~~2+ complex (Ru1)-encapsulated human heavy chain ferritin~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	[[Category: ~~Unreleased~~ Structures]]		</div>
	[[Category: Ferraro, G]]		<div class="pdbe-citations 8a2m" style="background-color:#fffaf0;"></div>
	[[Category: Merlino, A]]		== References ==
			<references/>
			__TOC__
			</StructureSection>
			[[Category: Homo sapiens]]
			[[Category: Large Structures]]
			[[Category: Ferraro G]]
			[[Category: Merlino A]]

OCA at 04:05, 13 July 2022

2022-07-13T04:05:42Z

← Older revision		Revision as of 04:05, 13 July 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 8a2m is ON HOLD		The entry 8a2m is ON HOLD until Paper Publication

	Authors: Ferraro, G., Merlino, A.		Authors: Ferraro, G., Merlino, A.

OCA: Protected "8a2m" [edit=sysop:move=sysop]

2022-06-15T04:05:44Z

Protected "8a2m" [edit=sysop:move=sysop]

← Older revision	Revision as of 04:05, 15 June 2022
(No difference)

OCA: New page: '''Unreleased structure''' The entry 8a2m is ON HOLD Authors: Ferraro, G., Merlino, A. Description: X-ray structure of Ru(bpy)3]2+ complex (Ru1)-encapsulated human heavy chain ferritin...

2022-06-15T04:05:43Z

New page: '''Unreleased structure''' The entry 8a2m is ON HOLD Authors: Ferraro, G., Merlino, A. Description: X-ray structure of Ru(bpy)3]2+ complex (Ru1)-encapsulated human heavy chain ferritin...

New page

'''Unreleased structure'''

The entry 8a2m is ON HOLD

Authors: Ferraro, G., Merlino, A.

Description: X-ray structure of Ru(bpy)3]2+ complex (Ru1)-encapsulated human heavy chain ferritin
[[Category: Unreleased Structures]]
[[Category: Ferraro, G]]
[[Category: Merlino, A]]