3h0t

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[[Image:3h0t.png|left|200px]]
 
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{{STRUCTURE_3h0t| PDB=3h0t | SCENE= }}
{{STRUCTURE_3h0t| PDB=3h0t | SCENE= }}
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===Hepcidin-Fab complex===
===Hepcidin-Fab complex===
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{{ABSTRACT_PUBMED_19553669}}
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{{ABSTRACT_PUBMED_19553669}}
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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:019553669</ref><references group="xtra"/>
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<ref group="xtra">PMID:019553669</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Li, V.]]
[[Category: Li, V.]]

Revision as of 10:55, 24 March 2013

Template:STRUCTURE 3h0t

Contents

Hepcidin-Fab complex

Template:ABSTRACT PUBMED 19553669

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

3h0t is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Jordan JB, Poppe L, Haniu M, Arvedson T, Syed R, Li V, Kohno H, Kim H, Schnier PD, Harvey TS, Miranda LP, Cheetham J, Sasu BJ. Hepcidin revisited, disulfide connectivity, dynamics, and structure. J Biol Chem. 2009 Sep 4;284(36):24155-67. Epub 2009 Jun 24. PMID:19553669 doi:10.1074/jbc.M109.017764
  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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