1als: Difference between revisions
New page: '''Theoretical Model''' The entry 1ALS is a Theoretical Model titled 'A MODELING STUDY OF THE ALPHA-SUBUNIT OF THE HUMAN HIGH-AFFINITY RECEPTOR FOR IMMUNOGLOBULIN-E'. [[Category:Theoreti... |
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{{Theoretical_model}} | |||
==A MODELING STUDY OF THE ALPHA-SUBUNIT OF THE HUMAN HIGH- AFFINITY RECEPTOR FOR IMMUNOGLOBULIN-E== | |||
<StructureSection load='1als' size='340' side='right'caption='[[1als]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALS FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1als FirstGlance], [https://www.ebi.ac.uk/pdbsum/1als PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1als ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The extracellular portion of the alpha-subunit of human high-affinity receptor for immunoglobulin-E (IgE), which contains two immunoglobulin (Ig) domains, was modeled on the basis of sequence similarity with antibody domains of known three-dimensional structure. Each receptor domain contains 86 amino acid residues, and both domains were modeled as bilayer structures. In both domains, one layer is made up of three anti-parallel beta-strands and the other of four strands, with the two layers linked by a disulfide bridge. The two domains show significant sequence similarity with each other (22 identities) and with the homologous domains of the murine and rat high-affinity receptors for IgE and the Fc gamma receptors from various species. Two plausible modes of association of the domains were considered: In the first, the two domains were positioned end-to-end, with essentially only longitudinal interactions between them; in the second, the molecule is more bent, with more lateral interactions between the two domains. The models will be useful in the design of protein engineering studies of this and homologous receptors to delineate the site of interaction with ligand. Furthermore, they may lend themselves as possible probes in crystallographic analyses by molecular replacement techniques. | |||
A modeling study of the alpha-subunit of human high-affinity receptor for immunoglobulin-E.,Padlan EA, Helm BA Receptor. 1992 Summer;2(2):129-44. PMID:1472946<ref>PMID:1472946</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1als" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Helm, B A]] | |||
[[Category: Padlan, E A]] | |||
Latest revision as of 12:46, 26 May 2021
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A MODELING STUDY OF THE ALPHA-SUBUNIT OF THE HUMAN HIGH- AFFINITY RECEPTOR FOR IMMUNOGLOBULIN-EA MODELING STUDY OF THE ALPHA-SUBUNIT OF THE HUMAN HIGH- AFFINITY RECEPTOR FOR IMMUNOGLOBULIN-E
Structural highlights
Publication Abstract from PubMedThe extracellular portion of the alpha-subunit of human high-affinity receptor for immunoglobulin-E (IgE), which contains two immunoglobulin (Ig) domains, was modeled on the basis of sequence similarity with antibody domains of known three-dimensional structure. Each receptor domain contains 86 amino acid residues, and both domains were modeled as bilayer structures. In both domains, one layer is made up of three anti-parallel beta-strands and the other of four strands, with the two layers linked by a disulfide bridge. The two domains show significant sequence similarity with each other (22 identities) and with the homologous domains of the murine and rat high-affinity receptors for IgE and the Fc gamma receptors from various species. Two plausible modes of association of the domains were considered: In the first, the two domains were positioned end-to-end, with essentially only longitudinal interactions between them; in the second, the molecule is more bent, with more lateral interactions between the two domains. The models will be useful in the design of protein engineering studies of this and homologous receptors to delineate the site of interaction with ligand. Furthermore, they may lend themselves as possible probes in crystallographic analyses by molecular replacement techniques. A modeling study of the alpha-subunit of human high-affinity receptor for immunoglobulin-E.,Padlan EA, Helm BA Receptor. 1992 Summer;2(2):129-44. PMID:1472946[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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