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| - | [[Image:1exu.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1exu.png|left|200px]] |
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| | {{STRUCTURE_1exu| PDB=1exu | SCENE= }} | | {{STRUCTURE_1exu| PDB=1exu | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF THE HUMAN MHC-RELATED FC RECEPTOR'''
| + | ===CRYSTAL STRUCTURE OF THE HUMAN MHC-RELATED FC RECEPTOR=== |
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| - | ==Overview==
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| - | The neonatal Fc receptor (FcRn) performs two distinct but related functions: transport of maternal immunoglobulin G (IgG) to pre- or neonatal mammals, thus providing passive immunity, and protection of IgG from normal serum protein catabolism. FcRn is related to class I MHC proteins but lacks a functional peptide binding groove. The crystal structure of human FcRn has been determined at 2.7 A resolution and compared to the previously described structure of rat FcRn [Burmeister et al. (1994) Nature 372, 336-343] and to the structures of MHC and MHC-related proteins. Human FcRn is structurally similar to the rat receptor but does not form receptor dimers in the crystals as observed in crystals of rat FcRn. The interaction between human FcRn and IgG was characterized by determining the binding stoichiometry using equilibrium gel filtration and by deriving binding affinities for the different human IgG subclasses using a surface plasmon resonance assay. Like rat and mouse FcRn, human FcRn interacts with IgG with a 2:1 receptor:ligand stoichiometry. The binding of human FcRn to the four human IgG subclasses shows subclass and allotype variations but no clear subclass affinity differences that correlate with serum half-lives. The structure of human FcRn and studies of its ligand binding are relevant to current efforts to use FcRn-mediated regulation of IgG half-life in serum to increase the lifetimes of antibody-based therapeutics. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10933786}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10933786 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10933786}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Jr., A P.West.]] | | [[Category: Jr., A P.West.]] |
| | [[Category: Immunoglobulin binding protein]] | | [[Category: Immunoglobulin binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:39:01 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:11:10 2008'' |
Revision as of 23:11, 30 June 2008
Template:STRUCTURE 1exu
CRYSTAL STRUCTURE OF THE HUMAN MHC-RELATED FC RECEPTOR
Template:ABSTRACT PUBMED 10933786
About this Structure
1EXU is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor(,)., West AP Jr, Bjorkman PJ, Biochemistry. 2000 Aug 15;39(32):9698-708. PMID:10933786
Page seeded by OCA on Tue Jul 1 02:11:10 2008
