1i1c

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[[Image:1i1c.gif|left|200px]]<br /><applet load="1i1c" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1i1c.gif|left|200px]]
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caption="1i1c, resolution 2.70&Aring;" />
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'''NON-FCRN BINDING FC FRAGMENT OF RAT IGG2A'''<br />
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{{Structure
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|PDB= 1i1c |SIZE=350|CAPTION= <scene name='initialview01'>1i1c</scene>, resolution 2.70&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''NON-FCRN BINDING FC FRAGMENT OF RAT IGG2A'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1I1C is a [[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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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11336709 11336709]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11336709 11336709]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: igg]]
[[Category: igg]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:44:14 2008''

Revision as of 09:44, 20 March 2008

Image:1i1c.gif


PDB ID 1i1c

Drag the structure with the mouse to rotate
, resolution 2.70Å
Coordinates: save as pdb, mmCIF, xml



NON-FCRN BINDING FC FRAGMENT OF RAT IGG2A


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

1I1C is a Single protein structure of sequence from Rattus norvegicus. 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

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