1m4f

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[[Image:1m4f.png|left|200px]]
 
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{{STRUCTURE_1m4f| PDB=1m4f | SCENE= }}
{{STRUCTURE_1m4f| PDB=1m4f | SCENE= }}
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===Solution Structure of Hepcidin-25===
===Solution Structure of Hepcidin-25===
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{{ABSTRACT_PUBMED_12138110}}
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{{ABSTRACT_PUBMED_12138110}}
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==Disease==
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[[http://www.uniprot.org/uniprot/HEPC_HUMAN HEPC_HUMAN]] Defects in HAMP are the cause of hemochromatosis type 2B (HFE2B) [MIM:[http://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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[[http://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>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:012138110</ref><references group="xtra"/>
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<ref group="xtra">PMID:012138110</ref><references group="xtra"/><references/>
[[Category: Fulton, D B.]]
[[Category: Fulton, D B.]]
[[Category: Ganz, T.]]
[[Category: Ganz, T.]]

Revision as of 19:34, 24 March 2013

Template:STRUCTURE 1m4f

Contents

Solution Structure of Hepcidin-25

Template:ABSTRACT PUBMED 12138110

Disease

[HEPC_HUMAN] Defects in HAMP are the cause of hemochromatosis type 2B (HFE2B) [MIM: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.[1][2][3][4][5]

Function

[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).[6] 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.[7]

About this Structure

1m4f is a 1 chain structure. Full experimental information is available from OCA.

Reference

  • Hunter HN, Fulton DB, Ganz T, Vogel HJ. The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. J Biol Chem. 2002 Oct 4;277(40):37597-603. Epub 2002 Jul 22. PMID:12138110 doi:10.1074/jbc.M205305200
  1. ↑ Biasiotto G, Belloli S, Ruggeri G, Zanella I, Gerardi G, Corrado M, Gobbi E, Albertini A, Arosio P. Identification of new mutations of the HFE, hepcidin, and transferrin receptor 2 genes by denaturing HPLC analysis of individuals with biochemical indications of iron overload. Clin Chem. 2003 Dec;49(12):1981-8. PMID:14633868 doi:10.1373/clinchem.2003.023440
  2. ↑ Merryweather-Clarke AT, Cadet E, Bomford A, Capron D, Viprakasit V, Miller A, McHugh PJ, Chapman RW, Pointon JJ, Wimhurst VL, Livesey KJ, Tanphaichitr V, Rochette J, Robson KJ. Digenic inheritance of mutations in HAMP and HFE results in different types of haemochromatosis. Hum Mol Genet. 2003 Sep 1;12(17):2241-7. Epub 2003 Jul 15. PMID:12915468 doi:http://dx.doi.org/10.1093/hmg/ddg225
  3. ↑ Roetto A, Daraio F, Porporato P, Caruso R, Cox TM, Cazzola M, Gasparini P, Piperno A, Camaschella C. Screening hepcidin for mutations in juvenile hemochromatosis: identification of a new mutation (C70R). Blood. 2004 Mar 15;103(6):2407-9. Epub 2003 Nov 20. PMID:14630809 doi:10.1182/blood-2003-10-3390
  4. ↑ Jacolot S, Le Gac G, Scotet V, Quere I, Mura C, Ferec C. HAMP as a modifier gene that increases the phenotypic expression of the HFE pC282Y homozygous genotype. Blood. 2004 Apr 1;103(7):2835-40. Epub 2003 Dec 11. PMID:14670915 doi:10.1182/blood-2003-10-3366
  5. ↑ Delatycki MB, Allen KJ, Gow P, MacFarlane J, Radomski C, Thompson J, Hayden MR, Goldberg YP, Samuels ME. A homozygous HAMP mutation in a multiply consanguineous family with pseudo-dominant juvenile hemochromatosis. Clin Genet. 2004 May;65(5):378-83. PMID:15099344 doi:10.1111/j.0009-9163.2004.00254.x
  6. ↑ Krause A, Neitz S, Magert HJ, Schulz A, Forssmann WG, Schulz-Knappe P, Adermann K. LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity. FEBS Lett. 2000 Sep 1;480(2-3):147-50. PMID:11034317
  7. ↑ Krause A, Neitz S, Magert HJ, Schulz A, Forssmann WG, Schulz-Knappe P, Adermann K. LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity. FEBS Lett. 2000 Sep 1;480(2-3):147-50. PMID:11034317

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