1rpq
From Proteopedia
(New page: 200px<br /> <applet load="1rpq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rpq, resolution 3.00Å" /> '''High Affinity IgE R...) |
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| - | [[Image:1rpq.gif|left|200px]]<br /> | + | [[Image:1rpq.gif|left|200px]]<br /><applet load="1rpq" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1rpq" size=" | + | |
caption="1rpq, resolution 3.00Å" /> | caption="1rpq, resolution 3.00Å" /> | ||
'''High Affinity IgE Receptor (alpha chain) Complexed with Tight-Binding E131 'zeta' Peptide from Phage Display'''<br /> | '''High Affinity IgE Receptor (alpha chain) Complexed with Tight-Binding E131 'zeta' Peptide from Phage Display'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Two structurally distinct classes of peptides were recently identified by | + | 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== | ==About this Structure== | ||
| - | 1RPQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NDG, SO4 and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RPQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NDG:'>NDG</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Eigenbrot, C.]] | [[Category: Eigenbrot, C.]] | ||
| - | [[Category: Fairbrother, W | + | [[Category: Fairbrother, W J.]] |
| - | [[Category: Lowman, H | + | [[Category: Lowman, H B.]] |
| - | [[Category: Nakamura, G | + | [[Category: Nakamura, G R.]] |
| - | [[Category: Reynolds, M | + | [[Category: Reynolds, M E.]] |
[[Category: Stamos, J.]] | [[Category: Stamos, J.]] | ||
| - | [[Category: Starovasnik, M | + | [[Category: Starovasnik, M A.]] |
| - | [[Category: Yin, J | + | [[Category: Yin, J P.]] |
[[Category: CIT]] | [[Category: CIT]] | ||
[[Category: NDG]] | [[Category: NDG]] | ||
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[[Category: receptor/peptide complex]] | [[Category: receptor/peptide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:17 2008'' |
Revision as of 12:53, 21 February 2008
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High Affinity IgE Receptor (alpha chain) Complexed with Tight-Binding E131 'zeta' Peptide from Phage Display
Overview
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
1RPQ is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 14:53:17 2008
