1de4
From Proteopedia
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|PDB= 1de4 |SIZE=350|CAPTION= <scene name='initialview01'>1de4</scene>, resolution 2.80Å | |PDB= 1de4 |SIZE=350|CAPTION= <scene name='initialview01'>1de4</scene>, resolution 2.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1a6z|1A6Z]], [[1cx8|1CX8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1de4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1de4 OCA], [http://www.ebi.ac.uk/pdbsum/1de4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1de4 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
HFE is related to major histocompatibility complex (MHC) class I proteins and is mutated in the iron-overload disease hereditary haemochromatosis. HFE binds to the transferrin receptor (TfR), a receptor by which cells acquire iron-loaded transferrin. The 2.8 A crystal structure of a complex between the extracellular portions of HFE and TfR shows two HFE molecules which grasp each side of a twofold symmetric TfR dimer. On a cell membrane containing both proteins, HFE would 'lie down' parallel to the membrane, such that the HFE helices that delineate the counterpart of the MHC peptide-binding groove make extensive contacts with helices in the TfR dimerization domain. The structures of TfR alone and complexed with HFE differ in their domain arrangement and dimer interfaces, providing a mechanism for communicating binding events between TfR chains. The HFE-TfR complex suggests a binding site for transferrin on TfR and sheds light upon the function of HFE in regulating iron homeostasis. | HFE is related to major histocompatibility complex (MHC) class I proteins and is mutated in the iron-overload disease hereditary haemochromatosis. HFE binds to the transferrin receptor (TfR), a receptor by which cells acquire iron-loaded transferrin. The 2.8 A crystal structure of a complex between the extracellular portions of HFE and TfR shows two HFE molecules which grasp each side of a twofold symmetric TfR dimer. On a cell membrane containing both proteins, HFE would 'lie down' parallel to the membrane, such that the HFE helices that delineate the counterpart of the MHC peptide-binding groove make extensive contacts with helices in the TfR dimerization domain. The structures of TfR alone and complexed with HFE differ in their domain arrangement and dimer interfaces, providing a mechanism for communicating binding events between TfR chains. The HFE-TfR complex suggests a binding site for transferrin on TfR and sheds light upon the function of HFE in regulating iron homeostasis. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Hemochromatosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=235200 235200]], Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]], Porphyria variegata OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=235200 235200]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Bjorkman, P J.]] | [[Category: Bjorkman, P J.]] | ||
[[Category: Lebron, J A.]] | [[Category: Lebron, J A.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: NAG]] | ||
[[Category: hereditary hemochromatosis]] | [[Category: hereditary hemochromatosis]] | ||
[[Category: hfe]] | [[Category: hfe]] | ||
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[[Category: transferrin receptor]] | [[Category: transferrin receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:39:48 2008'' |
Revision as of 16:39, 30 March 2008
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| , resolution 2.80Å | |||||||
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| Ligands: | , , | ||||||
| Related: | 1A6Z, 1CX8
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HEMOCHROMATOSIS PROTEIN HFE COMPLEXED WITH TRANSFERRIN RECEPTOR
Overview
HFE is related to major histocompatibility complex (MHC) class I proteins and is mutated in the iron-overload disease hereditary haemochromatosis. HFE binds to the transferrin receptor (TfR), a receptor by which cells acquire iron-loaded transferrin. The 2.8 A crystal structure of a complex between the extracellular portions of HFE and TfR shows two HFE molecules which grasp each side of a twofold symmetric TfR dimer. On a cell membrane containing both proteins, HFE would 'lie down' parallel to the membrane, such that the HFE helices that delineate the counterpart of the MHC peptide-binding groove make extensive contacts with helices in the TfR dimerization domain. The structures of TfR alone and complexed with HFE differ in their domain arrangement and dimer interfaces, providing a mechanism for communicating binding events between TfR chains. The HFE-TfR complex suggests a binding site for transferrin on TfR and sheds light upon the function of HFE in regulating iron homeostasis.
About this Structure
1DE4 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor., Bennett MJ, Lebron JA, Bjorkman PJ, Nature. 2000 Jan 6;403(6765):46-53. PMID:10638746
Page seeded by OCA on Sun Mar 30 19:39:48 2008
