1rpq
From Proteopedia
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|PDB= 1rpq |SIZE=350|CAPTION= <scene name='initialview01'>1rpq</scene>, resolution 3.00Å | |PDB= 1rpq |SIZE=350|CAPTION= <scene name='initialview01'>1rpq</scene>, resolution 3.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4 | + | |LIGAND= <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=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= FCER1A, FCE1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= FCER1A, FCE1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1kco|1KCO]], [[1f2q|1F2Q]], [[1f6a|1F6A]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rpq OCA], [http://www.ebi.ac.uk/pdbsum/1rpq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rpq RCSB]</span> | ||
}} | }} | ||
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[[Category: Starovasnik, M A.]] | [[Category: Starovasnik, M A.]] | ||
[[Category: Yin, J P.]] | [[Category: Yin, J P.]] | ||
| - | [[Category: CIT]] | ||
| - | [[Category: NDG]] | ||
| - | [[Category: SO4]] | ||
[[Category: receptor/peptide complex]] | [[Category: receptor/peptide complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:31:17 2008'' |
Revision as of 20:31, 30 March 2008
| |||||||
| , resolution 3.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Gene: | FCER1A, FCE1A (Homo sapiens) | ||||||
| Related: | 1KCO, 1F2Q, 1F6A
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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