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1j87

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Revision as of 09:53, 4 October 2017

HUMAN HIGH AFFINITY FC RECEPTOR FC(EPSILON)RI(ALPHA), HEXAGONAL CRYSTAL FORM 1

Structural highlights

1j87 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:	, , ,
Related:	1f2q, 1f6a, 1j86, 1j88, 1j89
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

We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments. This database of structures shows no change in the overall shape of the molecule, as the angle between domains 1 and 2 (D1 and D2) varies little across the ensemble. However, the receptor has local conformational variability in the C' strand of D2 and in the BC loop of D1. In every crystal form, a residue inserts between tryptophan residues 87 and 110, mimicking the position of a proline from the IgE ligand. The different crystal forms reveal a distribution of carbohydrates lining the front and back surfaces of the structure. An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site. The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.

The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.,Garman SC, Sechi S, Kinet JP, Jardetzky TS J Mol Biol. 2001 Aug 31;311(5):1049-62. PMID:11531339^[1]

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

References

↑ Garman SC, Sechi S, Kinet JP, Jardetzky TS. The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms. J Mol Biol. 2001 Aug 31;311(5):1049-62. PMID:11531339 doi:10.1006/jmbi.2001.4929

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/1j87"

@@ Line 1: / Line 1: @@
 ==HUMAN HIGH AFFINITY FC RECEPTOR FC(EPSILON)RI(ALPHA), HEXAGONAL CRYSTAL FORM 1==
 <StructureSection load='1j87' size='340' side='right' caption='[[1j87]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f2q|1f2q]], [[1f6a|1f6a]], [[1j86|1j86]], [[1j88|1j88]], [[1j89|1j89]]</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=1j87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j87 OCA], [http://pdbe.org/1j87 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j87 RCSB], [http://www.ebi.ac.uk/pdbsum/1j87 PDBsum]</span></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=1j87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j87 OCA], [http://pdbe.org/1j87 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j87 RCSB], [http://www.ebi.ac.uk/pdbsum/1j87 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j87 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1j87 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1j87

From Proteopedia

Revision as of 09:53, 4 October 2017

HUMAN HIGH AFFINITY FC RECEPTOR FC(EPSILON)RI(ALPHA), HEXAGONAL CRYSTAL FORM 1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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