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==THREE-DIMENSIONAL THEORETICAL MODEL OF THE LIGAND BINDING DOMAIN OF THE HUMAN B CELL RECPTOR CD40== | |||
<StructureSection load='1cdf' size='340' side='right' caption='[[1cdf]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CDF FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cdf FirstGlance], [http://www.ebi.ac.uk/pdbsum/1cdf PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The interaction between the human B cell receptor CD40 and its ligand on T cells is critical for B cell proliferation and the regulation of humoral immune responses. CD40 is a member of the tumor necrosis factor receptor (TNFR) family. We report here the construction and analysis of a detailed three-dimensional model of the TNFR-homologous extracellular region of CD40. This study provides an example for structure-based model building in the presence of low sequence similarity. The assessment of model quality and sequence-structure compatibility is emphasized, and limitations of the model are discussed. The current CD40 model predicts structural details beyond the backbone level. Features of the CD40 ligand binding site are discussed in conjunction with the results of a previous mutagenesis study. | |||
Construction and analysis of a detailed three-dimensional model of the ligand binding domain of the human B cell receptor CD40.,Bajorath J, Aruffo A Proteins. 1997 Jan;27(1):59-70. PMID:9037712<ref>PMID:9037712</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bajorath, J]] | [[Category: Bajorath, J]] | ||
Revision as of 15:05, 18 December 2014
THREE-DIMENSIONAL THEORETICAL MODEL OF THE LIGAND BINDING DOMAIN OF THE HUMAN B CELL RECPTOR CD40THREE-DIMENSIONAL THEORETICAL MODEL OF THE LIGAND BINDING DOMAIN OF THE HUMAN B CELL RECPTOR CD40
Structural highlights
Publication Abstract from PubMedThe interaction between the human B cell receptor CD40 and its ligand on T cells is critical for B cell proliferation and the regulation of humoral immune responses. CD40 is a member of the tumor necrosis factor receptor (TNFR) family. We report here the construction and analysis of a detailed three-dimensional model of the TNFR-homologous extracellular region of CD40. This study provides an example for structure-based model building in the presence of low sequence similarity. The assessment of model quality and sequence-structure compatibility is emphasized, and limitations of the model are discussed. The current CD40 model predicts structural details beyond the backbone level. Features of the CD40 ligand binding site are discussed in conjunction with the results of a previous mutagenesis study. Construction and analysis of a detailed three-dimensional model of the ligand binding domain of the human B cell receptor CD40.,Bajorath J, Aruffo A Proteins. 1997 Jan;27(1):59-70. PMID:9037712[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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