4zne

From Proteopedia

(Difference between revisions)

Current revision

IgG1 Fc-FcgammaRI ecd complex

Structural highlights

4zne is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.42Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FCGR1_HUMAN High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

The three-dimensional structure of a human IgG1 Fc fragment bound to wild-type human FcgammaRI is reported. The structure of the corresponding complex was solved at a resolution of 2.4 A using molecular replacement; this is the highest resolution achieved for an unmutated FcgammaRI molecule. This study highlights the critical structural and functional role played by the second extracellular subdomain of FcgammaRI. It also explains the long-known major energetic contribution of the Fc `LLGG' motif at positions 234-237, and particularly of Leu235, via a `lock-and-key' mechanism. Finally, a previously held belief is corrected and a differing view is offered on the recently proposed direct role of Fc carbohydrates in the corresponding interaction. Structural evidence is provided that such glycan-related effects are strictly indirect.

Structural insights into the interaction of human IgG1 with FcgammaRI: no direct role of glycans in binding.,Oganesyan V, Mazor Y, Yang C, Cook KE, Woods RM, Ferguson A, Bowen MA, Martin T, Zhu J, Wu H, Dall'Acqua WF Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2354-61. doi:, 10.1107/S1399004715018015. Epub 2015 Oct 31. PMID:26527150^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ van Vugt MJ, Heijnen AF, Capel PJ, Park SY, Ra C, Saito T, Verbeek JS, van de Winkel JG. FcR gamma-chain is essential for both surface expression and function of human Fc gamma RI (CD64) in vivo. Blood. 1996 May 1;87(9):3593-9. PMID:8611682
↑ Ernst LK, Duchemin AM, Miller KL, Anderson CL. Molecular characterization of six variant Fcgamma receptor class I (CD64) transcripts. Mol Immunol. 1998 Oct;35(14-15):943-54. PMID:9881690
↑ van Vugt MJ, Kleijmeer MJ, Keler T, Zeelenberg I, van Dijk MA, Leusen JH, Geuze HJ, van de Winkel JG. The FcgammaRIa (CD64) ligand binding chain triggers major histocompatibility complex class II antigen presentation independently of its associated FcR gamma-chain. Blood. 1999 Jul 15;94(2):808-17. PMID:10397749
↑ Edberg JC, Yee AM, Rakshit DS, Chang DJ, Gokhale JA, Indik ZK, Schreiber AD, Kimberly RP. The cytoplasmic domain of human FcgammaRIa alters the functional properties of the FcgammaRI.gamma-chain receptor complex. J Biol Chem. 1999 Oct 15;274(42):30328-33. PMID:10514529
↑ Oganesyan V, Mazor Y, Yang C, Cook KE, Woods RM, Ferguson A, Bowen MA, Martin T, Zhu J, Wu H, Dall'Acqua WF. Structural insights into the interaction of human IgG1 with FcgammaRI: no direct role of glycans in binding. Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2354-61. doi:, 10.1107/S1399004715018015. Epub 2015 Oct 31. PMID:26527150 doi:http://dx.doi.org/10.1107/S1399004715018015

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4zne"

Categories: Homo sapiens | Large Structures | Dall'Acqua WF | Oganesyan VY

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4zne is ON HOLD
+==IgG1 Fc-FcgammaRI ecd complex==
+<StructureSection load='4zne' size='340' side='right'caption='[[4zne]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4zne]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZNE FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.42&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zne OCA], [https://pdbe.org/4zne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zne RCSB], [https://www.ebi.ac.uk/pdbsum/4zne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zne ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FCGR1_HUMAN FCGR1_HUMAN] High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses.<ref>PMID:8611682</ref> <ref>PMID:9881690</ref> <ref>PMID:10397749</ref> <ref>PMID:10514529</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The three-dimensional structure of a human IgG1 Fc fragment bound to wild-type human FcgammaRI is reported. The structure of the corresponding complex was solved at a resolution of 2.4 A using molecular replacement; this is the highest resolution achieved for an unmutated FcgammaRI molecule. This study highlights the critical structural and functional role played by the second extracellular subdomain of FcgammaRI. It also explains the long-known major energetic contribution of the Fc `LLGG' motif at positions 234-237, and particularly of Leu235, via a `lock-and-key' mechanism. Finally, a previously held belief is corrected and a differing view is offered on the recently proposed direct role of Fc carbohydrates in the corresponding interaction. Structural evidence is provided that such glycan-related effects are strictly indirect.
-Authors: Oganesyan, V.Y., Dall'Acqua, W.F.
+Structural insights into the interaction of human IgG1 with FcgammaRI: no direct role of glycans in binding.,Oganesyan V, Mazor Y, Yang C, Cook KE, Woods RM, Ferguson A, Bowen MA, Martin T, Zhu J, Wu H, Dall'Acqua WF Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2354-61. doi:, 10.1107/S1399004715018015. Epub 2015 Oct 31. PMID:26527150<ref>PMID:26527150</ref>
-Description: IgG1 Fc-FcgammaRI ecd complex
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Dall'Acqua, W.F]]
+<div class="pdbe-citations 4zne" style="background-color:#fffaf0;"></div>
-[[Category: Oganesyan, V.Y]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Dall'Acqua WF]]
+[[Category: Oganesyan VY]]

4zne

From Proteopedia

Current revision

IgG1 Fc-FcgammaRI ecd complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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