This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1i1a
From Proteopedia
(New page: 200px<br /><applet load="1i1a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i1a, resolution 2.80Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1i1a.gif|left|200px]]<br /><applet load="1i1a" size=" | + | [[Image:1i1a.gif|left|200px]]<br /><applet load="1i1a" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i1a, resolution 2.80Å" /> | caption="1i1a, resolution 2.80Å" /> | ||
'''CRYSTAL STRUCTURE OF THE NEONATAL FC RECEPTOR COMPLEXED WITH A HETERODIMERIC FC'''<br /> | '''CRYSTAL STRUCTURE OF THE NEONATAL FC RECEPTOR COMPLEXED WITH A HETERODIMERIC FC'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The neonatal Fc receptor (FcRn) transports immunoglobulin G (IgG) across | + | The neonatal Fc receptor (FcRn) transports immunoglobulin G (IgG) across epithelia, binding IgG in acidic vesicles (pH < or = 6.5) and releasing IgG in the blood at pH 7.4. Well-ordered FcRn/Fc crystals are prevented by the formation of "oligomeric ribbons" of FcRn dimers bridged by Fc homodimers, thus we crystallized a 1:1 complex between rat FcRn and a heterodimeric Fc containing only one FcRn binding site. The 2.8 A complex structure demonstrates that FcRn uses its alpha2 and beta2-microglobulin domains and carbohydrate to interact with the Fc C(gamma)2-C(gamma)3 interface. The structure reveals conformational changes in Fc and three titratable salt bridges that confer pH-dependent binding, and can be used to guide rational design of therapeutic IgGs with longer serum half-lives. |
==About this Structure== | ==About this Structure== | ||
| - | 1I1A 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 NDG, NAG and CYS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1I1A 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=NDG:'>NDG</scene>, <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=CYS:'>CYS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1A OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Bjorkman, P | + | [[Category: Bjorkman, P J.]] |
[[Category: Gan, L.]] | [[Category: Gan, L.]] | ||
| - | [[Category: Jr., A | + | [[Category: Jr., A P.West.]] |
| - | [[Category: Martin, W | + | [[Category: Martin, W L.]] |
[[Category: CYS]] | [[Category: CYS]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
| Line 23: | Line 23: | ||
[[Category: mhc class i fold]] | [[Category: mhc class i fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:56 2008'' |
Revision as of 11:06, 21 February 2008
|
CRYSTAL STRUCTURE OF THE NEONATAL FC RECEPTOR COMPLEXED WITH A HETERODIMERIC FC
Overview
The neonatal Fc receptor (FcRn) transports immunoglobulin G (IgG) across epithelia, binding IgG in acidic vesicles (pH < or = 6.5) and releasing IgG in the blood at pH 7.4. Well-ordered FcRn/Fc crystals are prevented by the formation of "oligomeric ribbons" of FcRn dimers bridged by Fc homodimers, thus we crystallized a 1:1 complex between rat FcRn and a heterodimeric Fc containing only one FcRn binding site. The 2.8 A complex structure demonstrates that FcRn uses its alpha2 and beta2-microglobulin domains and carbohydrate to interact with the Fc C(gamma)2-C(gamma)3 interface. The structure reveals conformational changes in Fc and three titratable salt bridges that confer pH-dependent binding, and can be used to guide rational design of therapeutic IgGs with longer serum half-lives.
About this Structure
1I1A is a Protein complex structure of sequences from Rattus norvegicus with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure at 2.8 A of an FcRn/heterodimeric Fc complex: mechanism of pH-dependent binding., Martin WL, West AP Jr, Gan L, Bjorkman PJ, Mol Cell. 2001 Apr;7(4):867-77. PMID:11336709
Page seeded by OCA on Thu Feb 21 13:06:56 2008
