This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 15: | Line 14: | ||
[[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]] | ||
| Line 27: | Line 26: | ||
[[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
|
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
