1f2q

From Proteopedia

(Difference between revisions)

Revision as of 09:45, 21 July 2021

CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR

Structural highlights

1f2q is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FCERA_HUMAN] Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Allergic responses result from the activation of mast cells by the human high-affinity IgE receptor. IgE-mediated allergic reactions may develop to a variety of environmental compounds, but the initiation of a response requires the binding of IgE to its high-affinity receptor. We have solved the X-ray crystal structure of the antibody-binding domains of the human IgE receptor at 2.4 A resolution. The structure reveals a highly bent arrangement of immunoglobulin domains that form an extended convex surface of interaction with IgE. A prominent loop that confers specificity for IgE molecules extends from the receptor surface near an unusual arrangement of four exposed tryptophans. The crystal structure of the IgE receptor provides a foundation for the development of new therapeutic approaches to allergy treatment.

Crystal structure of the human high-affinity IgE receptor.,Garman SC, Kinet JP, Jardetzky TS Cell. 1998 Dec 23;95(7):951-61. PMID:9875849^[1]

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

References

↑ Garman SC, Kinet JP, Jardetzky TS. Crystal structure of the human high-affinity IgE receptor. Cell. 1998 Dec 23;95(7):951-61. PMID:9875849

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1f2q"

@@ Line 3: / Line 3: @@
 <StructureSection load='1f2q' size='340' side='right'caption='[[1f2q]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1f2q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F2Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1f2q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2q OCA], [http://pdbe.org/1f2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f2q RCSB], [http://www.ebi.ac.uk/pdbsum/1f2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2q ProSAT]</span></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=1f2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2q OCA], [https://pdbe.org/1f2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2q RCSB], [https://www.ebi.ac.uk/pdbsum/1f2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2q ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FCERA_HUMAN FCERA_HUMAN]] Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines.
+[[https://www.uniprot.org/uniprot/FCERA_HUMAN FCERA_HUMAN]] Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1f2q

From Proteopedia

Revision as of 09:45, 21 July 2021

CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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