3h0t

From Proteopedia

(Difference between revisions)

Current revision

Hepcidin-Fab complex

Structural highlights

3h0t is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.89Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Hepcidin is a tightly folded 25-residue peptide hormone containing four disulfide bonds, which has been shown to act as the principal regulator of iron homeostasis in vertebrates. We used multiple techniques to demonstrate a disulfide bonding pattern for hepcidin different from that previously published. All techniques confirmed the following disulfide bond connectivity: Cys(1)-Cys(8), Cys(3)-Cys(6), Cys(2)-Cys(4), and Cys(5)-Cys(7). NMR studies reveal a new model for hepcidin that, at ambient temperatures, interconverts between two different conformations, which could be individually resolved by temperature variation. Using these methods, the solution structure of hepcidin was determined at 325 and 253 K in supercooled water. X-ray analysis of a co-crystal with Fab appeared to stabilize a hepcidin conformation similar to the high temperature NMR structure.

Hepcidin revisited, disulfide connectivity, dynamics, and structure.,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 J Biol Chem. 2009 Sep 4;284(36):24155-67. Epub 2009 Jun 24. PMID:19553669^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3h0t"

Categories: Homo sapiens | Large Structures | Li V | Syed R

@@ Line 1: / Line 1: @@
 ==Hepcidin-Fab complex==
-<StructureSection load='3h0t' size='340' side='right' caption='[[3h0t]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
+<StructureSection load='3h0t' size='340' side='right'caption='[[3h0t]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3h0t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H0T FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3h0t]] is a 3 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=3H0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H0T FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HAMP, HEPC, hepcidin, LEAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 1.89&#8491;</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=3h0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h0t OCA], [http://pdbe.org/3h0t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h0t RCSB], [http://www.ebi.ac.uk/pdbsum/3h0t PDBsum]</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=3h0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h0t OCA], [https://pdbe.org/3h0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h0t RCSB], [https://www.ebi.ac.uk/pdbsum/3h0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h0t ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[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>
+[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>
 == Function ==
-[[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>
+[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h0/3h0t_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h0/3h0t_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 31: / Line 32: @@
 ==See Also==
-*[[Antibody|Antibody]]
+*[[Antibody 3D structures|Antibody 3D structures]]
+*[[3D structures of human antibody|3D structures of human antibody]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Li, V]]
+[[Category: Large Structures]]
-[[Category: Syed, R]]
+[[Category: Li V]]
-[[Category: Antibiotic]]
+[[Category: Syed R]]
-[[Category: Antimicrobial]]
-[[Category: Cleavage on pair of basic residue]]
-[[Category: Disease mutation]]
-[[Category: Disulfide bond]]
-[[Category: Fungicide]]
-[[Category: Hormone]]
-[[Category: Immune system-antimicrobial protein complex]]
-[[Category: Peptide-fab complex]]
-[[Category: Secreted]]

3h0t

From Proteopedia

Current revision

Hepcidin-Fab complex

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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