1i1a: Difference between revisions

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-[[Image:1i1a.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF THE NEONATAL FC RECEPTOR COMPLEXED WITH A HETERODIMERIC FC==
-|PDB= 1i1a |SIZE=350|CAPTION= <scene name='initialview01'>1i1a</scene>, resolution 2.80&Aring;
+<StructureSection load='1i1a' size='340' side='right'caption='[[1i1a]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>
+<table><tr><td colspan='2'>[[1i1a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I1A FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1a OCA], [https://pdbe.org/1i1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i1a RCSB], [https://www.ebi.ac.uk/pdbsum/1i1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1a ProSAT]</span></td></tr>
-|RELATEDENTRY=[[3fru|3fru]], [[1fc1|1FC1]], [[1i1c|1i1c]]
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1a OCA], [http://www.ebi.ac.uk/pdbsum/1i1a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i1a RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/FCGRN_RAT FCGRN_RAT] Binds to the Fc region of monomeric immunoglobulins gamma. Mediates the selective uptake of IgG from milk and helps newborn animals to acquire passive immunity. IgG in the milk is bound at the apical surface of the intestinal epithelium. The resultant FcRn-IgG complexes are transcytosed across the intestinal epithelium and IgG is released from FcRn into blood or tissue fluids (By similarity).
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i1/1i1a_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1i1a ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The neonatal Fc receptor (FcRn) transports immunoglobulin G (IgG) across epithelia, binding IgG in acidic vesicles (pH &lt; 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.
-'''CRYSTAL STRUCTURE OF THE NEONATAL FC RECEPTOR COMPLEXED WITH A HETERODIMERIC FC'''
+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<ref>PMID:11336709</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1i1a" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-The neonatal Fc receptor (FcRn) transports immunoglobulin G (IgG) across epithelia, binding IgG in acidic vesicles (pH &lt; 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.
+*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-I1A is a [[Protein complex]] structure of sequences 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=1I1A OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-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: Protein complex]]
 [[Category: Rattus norvegicus]]
-[[Category: Bjorkman, P J.]]
+[[Category: Bjorkman PJ]]
-[[Category: Gan, L.]]
+[[Category: Gan L]]
-[[Category: Jr., A P.West.]]
+[[Category: Martin WL]]
-[[Category: Martin, W L.]]
+[[Category: West Jr AP]]
-[[Category: ig constant domain]]
-[[Category: mhc class i fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:13:14 2008''