1rpq: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
caption="1rpq, resolution 3.00&Aring;" />
caption="1rpq, resolution 3.00&Aring;" />
'''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, 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==
==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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RPQ OCA].  
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.J.]]
[[Category: Fairbrother, W J.]]
[[Category: Lowman, H.B.]]
[[Category: Lowman, H B.]]
[[Category: Nakamura, G.R.]]
[[Category: Nakamura, G R.]]
[[Category: Reynolds, M.E.]]
[[Category: Reynolds, M E.]]
[[Category: Stamos, J.]]
[[Category: Stamos, J.]]
[[Category: Starovasnik, M.A.]]
[[Category: Starovasnik, M A.]]
[[Category: Yin, J.P.]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:06:16 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:17 2008''