1m4e

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[[Image:1m4e.gif|left|200px]]
 
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==Solution Structure of Hepcidin-20==
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The line below this paragraph, containing "STRUCTURE_1m4e", creates the "Structure Box" on the page.
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<StructureSection load='1m4e' size='340' side='right'caption='[[1m4e]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1m4e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M4E FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4e OCA], [https://pdbe.org/1m4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m4e RCSB], [https://www.ebi.ac.uk/pdbsum/1m4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m4e ProSAT]</span></td></tr>
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{{STRUCTURE_1m4e| PDB=1m4e | SCENE= }}
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</table>
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== Disease ==
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'''Solution Structure of Hepcidin-20'''
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[https://www.uniprot.org/uniprot/HEPC_HUMAN HEPC_HUMAN] Defects in HAMP are the cause of hemochromatosis type 2B (HFE2B) [MIM:[https://omim.org/entry/613313 613313]; also known as juvenile hemochromatosis (JH). HFE2B is a disorder of iron metabolism with excess deposition of iron in the tissues, bronze skin pigmentation, hepatic cirrhosis, arthropathy and diabetes. The most common symptoms of hemochromatosis type 2 at presentation are hypogonadism and cardiomyopathy.<ref>PMID:14633868</ref> <ref>PMID:12915468</ref> <ref>PMID:14630809</ref> <ref>PMID:14670915</ref> <ref>PMID:15099344</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/HEPC_HUMAN HEPC_HUMAN] Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages (By similarity).<ref>PMID:11034317</ref> Has strong antimicrobial activity against E.coli ML35P N.cinerea and weaker against S.epidermidis, S.aureus and group b streptococcus bacteria. Active against the fungus C.albicans. No activity against P.aeruginosa.<ref>PMID:11034317</ref>
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==Overview==
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The antibacterial and antifungal peptide hepcidin (LEAP-1) is expressed in the liver. This circulating peptide has recently been found to also act as a signaling molecule in iron metabolism. As such, it plays an important role in hereditary hemochromatosis, a serious iron overload disease. In this study, we report the solution structures of the hepcidin-20 and -25 amino acid peptides determined by standard two-dimensional (1)H NMR spectroscopy. These small cysteine-rich peptides form a distorted beta-sheet with an unusual vicinal disulfide bridge found at the turn of the hairpin, which is probably of functional significance. Both peptides exhibit an overall amphipathic structure with six of the eight Cys involved in maintaining interstrand connectivity. Hepcidin-25 assumes major and minor conformations centered about the Pro residue near the N-terminal end. Further NMR diffusion studies indicate that hepcidin-20 exists as a monomer in solution, whereas hepcidin-25 readily aggregates, a property that may contribute to the different activities of the two peptides. The nuclear Overhauser enhancement spectroscopy spectra of the hepcidin-25 aggregates indicate an interface for peptide interactions that again involves the first five residues from the N-terminal end.
The antibacterial and antifungal peptide hepcidin (LEAP-1) is expressed in the liver. This circulating peptide has recently been found to also act as a signaling molecule in iron metabolism. As such, it plays an important role in hereditary hemochromatosis, a serious iron overload disease. In this study, we report the solution structures of the hepcidin-20 and -25 amino acid peptides determined by standard two-dimensional (1)H NMR spectroscopy. These small cysteine-rich peptides form a distorted beta-sheet with an unusual vicinal disulfide bridge found at the turn of the hairpin, which is probably of functional significance. Both peptides exhibit an overall amphipathic structure with six of the eight Cys involved in maintaining interstrand connectivity. Hepcidin-25 assumes major and minor conformations centered about the Pro residue near the N-terminal end. Further NMR diffusion studies indicate that hepcidin-20 exists as a monomer in solution, whereas hepcidin-25 readily aggregates, a property that may contribute to the different activities of the two peptides. The nuclear Overhauser enhancement spectroscopy spectra of the hepcidin-25 aggregates indicate an interface for peptide interactions that again involves the first five residues from the N-terminal end.
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==About this Structure==
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The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis.,Hunter HN, Fulton DB, Ganz T, Vogel HJ J Biol Chem. 2002 Oct 4;277(40):37597-603. Epub 2002 Jul 22. PMID:12138110<ref>PMID:12138110</ref>
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1M4E is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4E OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis., Hunter HN, Fulton DB, Ganz T, Vogel HJ, J Biol Chem. 2002 Oct 4;277(40):37597-603. Epub 2002 Jul 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12138110 12138110]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1m4e" style="background-color:#fffaf0;"></div>
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[[Category: Fulton, D B.]]
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== References ==
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[[Category: Ganz, T.]]
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<references/>
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[[Category: Hunter, H N.]]
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__TOC__
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[[Category: Vogel, H J.]]
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</StructureSection>
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[[Category: Beta-sheet]]
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[[Category: Homo sapiens]]
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[[Category: Hairpin loop]]
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[[Category: Large Structures]]
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[[Category: Strand-loop-strand]]
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[[Category: Fulton DB]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:37:01 2008''
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[[Category: Ganz T]]
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[[Category: Hunter HN]]
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[[Category: Vogel HJ]]

Current revision

Solution Structure of Hepcidin-20

PDB ID 1m4e

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