1frt

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(New page: 200px<br /><applet load="1frt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1frt, resolution 4.5&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1frt.gif|left|200px]]<br /><applet load="1frt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1frt, resolution 4.5&Aring;" />
caption="1frt, resolution 4.5&Aring;" />
'''CRYSTAL STRUCTURE OF THE COMPLEX OF RAT NEONATAL FC RECEPTOR WITH FC'''<br />
'''CRYSTAL STRUCTURE OF THE COMPLEX OF RAT NEONATAL FC RECEPTOR WITH FC'''<br />
==Overview==
==Overview==
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The neonatal Fc receptor (FcRn) transports maternal immunoglobulin G (IgG), to the bloodstream of the newborn. FcRn is structurally similar to class I, major histocompatibility complex (MHC) molecules, despite differences in, the ligands they bind (the Fc portion of IgG and antigenic peptides, respectively). A low-resolution crystal structure of the complex between, FcRn and Fc localizes the binding site for Fc to the side of FcRn, distinct from the tops of the alpha 1 and alpha 2 domains which serve as, the peptide and T-cell receptor binding sites in class I molecules. FcRn, binds to Fc at the interface between the Fc CH2 and CH3 domains, which, contains several histidine residues that could account for the sharply, pH-dependent FcRn/IgG interaction. A dimer of FcRn heterodimers observed, in the co-crystals and in the crystals of FcRn alone could be involved in, binding Fc, correlating with the 2:1 binding stoichiometry between FcRn, and IgG (ref. 4) and suggesting an unusual orientation of FcRn on the, membrane.
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The neonatal Fc receptor (FcRn) transports maternal immunoglobulin G (IgG) to the bloodstream of the newborn. FcRn is structurally similar to class I major histocompatibility complex (MHC) molecules, despite differences in the ligands they bind (the Fc portion of IgG and antigenic peptides, respectively). A low-resolution crystal structure of the complex between FcRn and Fc localizes the binding site for Fc to the side of FcRn, distinct from the tops of the alpha 1 and alpha 2 domains which serve as the peptide and T-cell receptor binding sites in class I molecules. FcRn binds to Fc at the interface between the Fc CH2 and CH3 domains, which contains several histidine residues that could account for the sharply pH-dependent FcRn/IgG interaction. A dimer of FcRn heterodimers observed in the co-crystals and in the crystals of FcRn alone could be involved in binding Fc, correlating with the 2:1 binding stoichiometry between FcRn and IgG (ref. 4) and suggesting an unusual orientation of FcRn on the membrane.
==About this Structure==
==About this Structure==
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1FRT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FRT OCA].
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1FRT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRT OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Bjorkman, P.J.]]
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[[Category: Bjorkman, P J.]]
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[[Category: Burmeister, W.P.]]
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[[Category: Burmeister, W P.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: complex (receptor/immunoglobulin)]]
[[Category: complex (receptor/immunoglobulin)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:12:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:01 2008''

Revision as of 10:42, 21 February 2008


1frt, resolution 4.5Å

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CRYSTAL STRUCTURE OF THE COMPLEX OF RAT NEONATAL FC RECEPTOR WITH FC

Overview

The neonatal Fc receptor (FcRn) transports maternal immunoglobulin G (IgG) to the bloodstream of the newborn. FcRn is structurally similar to class I major histocompatibility complex (MHC) molecules, despite differences in the ligands they bind (the Fc portion of IgG and antigenic peptides, respectively). A low-resolution crystal structure of the complex between FcRn and Fc localizes the binding site for Fc to the side of FcRn, distinct from the tops of the alpha 1 and alpha 2 domains which serve as the peptide and T-cell receptor binding sites in class I molecules. FcRn binds to Fc at the interface between the Fc CH2 and CH3 domains, which contains several histidine residues that could account for the sharply pH-dependent FcRn/IgG interaction. A dimer of FcRn heterodimers observed in the co-crystals and in the crystals of FcRn alone could be involved in binding Fc, correlating with the 2:1 binding stoichiometry between FcRn and IgG (ref. 4) and suggesting an unusual orientation of FcRn on the membrane.

About this Structure

1FRT is a Protein complex structure of sequences from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the complex of rat neonatal Fc receptor with Fc., Burmeister WP, Huber AH, Bjorkman PJ, Nature. 1994 Nov 24;372(6504):379-83. PMID:7969498

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