Document Detail


The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.
MedLine Citation:
PMID:  11531339     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments. This database of structures shows no change in the overall shape of the molecule, as the angle between domains 1 and 2 (D1 and D2) varies little across the ensemble. However, the receptor has local conformational variability in the C' strand of D2 and in the BC loop of D1. In every crystal form, a residue inserts between tryptophan residues 87 and 110, mimicking the position of a proline from the IgE ligand. The different crystal forms reveal a distribution of carbohydrates lining the front and back surfaces of the structure. An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site. The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
Authors:
S C Garman; S Sechi; J P Kinet; T S Jardetzky
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of molecular biology     Volume:  311     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2001 Aug 
Date Detail:
Created Date:  2001-09-04     Completed Date:  2001-09-27     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1049-62     Citation Subset:  IM    
Copyright Information:
Copyright 2001 Academic Press.
Affiliation:
Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Twinbrook II, 12441 Parklawn Drive, Rockville, MD 20852, USA. garman@alpha.niaid.nih.gov
Data Bank Information
Bank Name/Acc. No.:
PDB/1F2Q;  1F6A;  1J86;  1J87;  1J88;  1J89
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MeSH Terms
Descriptor/Qualifier:
Binding Sites
Carbohydrate Metabolism
Crystallization
Crystallography, X-Ray
Databases as Topic
Drug Design
Glycoproteins / chemistry,  metabolism
Humans
Immunoglobulin E / chemistry,  metabolism
Immunoglobulin Heavy Chains / chemistry,  metabolism
Ligands
Models, Molecular
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Receptors, IgE / chemistry*,  metabolism*
Thermodynamics
Chemical
Reg. No./Substance:
0/Glycoproteins; 0/Immunoglobulin Heavy Chains; 0/Ligands; 0/Receptors, IgE; 37341-29-0/Immunoglobulin E

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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