1i1c: Difference between revisions
New page: left|200px<br /><applet load="1i1c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i1c, resolution 2.70Å" /> '''NON-FCRN BINDING FC ... |
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[[Image:1i1c.gif|left|200px]]<br /><applet load="1i1c" size=" | [[Image:1i1c.gif|left|200px]]<br /><applet load="1i1c" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1i1c, resolution 2.70Å" /> | caption="1i1c, resolution 2.70Å" /> | ||
'''NON-FCRN BINDING FC FRAGMENT OF RAT IGG2A'''<br /> | '''NON-FCRN BINDING FC FRAGMENT OF RAT IGG2A'''<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== | ||
1I1C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | 1I1C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1C OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[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: fc]] | [[Category: fc]] | ||
[[Category: igg]] | [[Category: igg]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:57 2008'' | ||
Revision as of 14:06, 21 February 2008
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NON-FCRN BINDING FC FRAGMENT OF RAT IGG2A
OverviewOverview
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 StructureAbout this Structure
1I1C is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
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
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