1rpq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:26, 9 October 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1rpq.gif|left|200px]]
 
-
<!--
+
==High Affinity IgE Receptor (alpha chain) Complexed with Tight-Binding E131 'zeta' Peptide from Phage Display==
-
The line below this paragraph, containing "STRUCTURE_1rpq", creates the "Structure Box" on the page.
+
<StructureSection load='1rpq' size='340' side='right'caption='[[1rpq]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1rpq]] is a 8 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=1RPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RPQ FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-
-->
+
<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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
{{STRUCTURE_1rpq| PDB=1rpq | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rpq OCA], [https://pdbe.org/1rpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rpq RCSB], [https://www.ebi.ac.uk/pdbsum/1rpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rpq ProSAT]</span></td></tr>
-
 
+
</table>
-
'''High Affinity IgE Receptor (alpha chain) Complexed with Tight-Binding E131 'zeta' Peptide from Phage Display'''
+
== Function ==
-
 
+
[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 ==
-
==Overview==
+
[[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/rp/1rpq_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=1rpq ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
Two structurally distinct classes of peptides were recently identified by phage display that bind the high-affinity IgE receptor, FcepsilonRI, and block IgE binding and subsequent receptor activation. Both classes adopt highly stable structures in solution, one forming a beta hairpin, with the other forming a helical "zeta" structure. Despite these differences, the two classes bind competitively to the same site on the receptor. Structural analyses of both peptide-receptor complexes by NMR spectroscopy and/or X-ray crystallography reveal that the unrelated peptide scaffolds have nevertheless converged to present a similar three-dimensional surface to interact with FcepsilonRI and that their modes of interaction share a key feature of the IgE-FcepsilonRI complex, the proline/tryptophan sandwich.
Two structurally distinct classes of peptides were recently identified by phage display that bind the high-affinity IgE receptor, FcepsilonRI, and block IgE binding and subsequent receptor activation. Both classes adopt highly stable structures in solution, one forming a beta hairpin, with the other forming a helical "zeta" structure. Despite these differences, the two classes bind competitively to the same site on the receptor. Structural analyses of both peptide-receptor complexes by NMR spectroscopy and/or X-ray crystallography reveal that the unrelated peptide scaffolds have nevertheless converged to present a similar three-dimensional surface to interact with FcepsilonRI and that their modes of interaction share a key feature of the IgE-FcepsilonRI complex, the proline/tryptophan sandwich.
-
==About this Structure==
+
Convergent recognition of the IgE binding site on the high-affinity IgE receptor.,Stamos J, Eigenbrot C, Nakamura GR, Reynolds ME, Yin J, Lowman HB, Fairbrother WJ, Starovasnik MA Structure. 2004 Jul;12(7):1289-301. PMID:15242605<ref>PMID:15242605</ref>
-
1RPQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPQ OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Convergent recognition of the IgE binding site on the high-affinity IgE receptor., Stamos J, Eigenbrot C, Nakamura GR, Reynolds ME, Yin J, Lowman HB, Fairbrother WJ, Starovasnik MA, Structure. 2004 Jul;12(7):1289-301. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15242605 15242605]
+
</div>
 +
<div class="pdbe-citations 1rpq" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Eigenbrot, C.]]
+
[[Category: Eigenbrot C]]
-
[[Category: Fairbrother, W J.]]
+
[[Category: Fairbrother WJ]]
-
[[Category: Lowman, H B.]]
+
[[Category: Lowman HB]]
-
[[Category: Nakamura, G R.]]
+
[[Category: Nakamura GR]]
-
[[Category: Reynolds, M E.]]
+
[[Category: Reynolds ME]]
-
[[Category: Stamos, J.]]
+
[[Category: Stamos J]]
-
[[Category: Starovasnik, M A.]]
+
[[Category: Starovasnik MA]]
-
[[Category: Yin, J P.]]
+
[[Category: Yin JP]]
-
[[Category: Receptor/peptide complex]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:45:58 2008''
+

Current revision

High Affinity IgE Receptor (alpha chain) Complexed with Tight-Binding E131 'zeta' Peptide from Phage Display

PDB ID 1rpq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rpq"
Personal tools