1de4: Difference between revisions
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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. | ||
==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: 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'' | ||
