1cda: Difference between revisions
New page: '''Theoretical Model''' The entry 1CDA is a Theoretical Model titled 'A 3-DIMENSIONAL MODEL FOR THE CD40 LIGAND REVEALS A CLOSE SIMILARITY TO THE TUMOR NECROSIS FACTORS'. [[Category:Theo... |
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{{Theoretical_model}} | |||
==A 3-DIMENSIONAL MODEL FOR THE CD40 LIGAND REVEALS A CLOSE SIMILARITY TO THE TUMOR NECROSIS FACTORS== | |||
<StructureSection load='1cda' size='340' side='right'caption='[[1cda]]' 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=1CDA 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=1cda FirstGlance], [https://www.ebi.ac.uk/pdbsum/1cda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cda ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Based on the similarity in primary structure between the newly characterized ligand for CD40 (CD40L) and the tumor necrosis factors (TNFs), we have modeled a detailed 3-D structure for CD40L. We used the known structure of TNF alpha as a template for the generation of the CD40L model. The soundness of the model-building algorithms was verified by constructing a 3-D model of TNF beta and comparing it to its crystallographically determined structure. The CD40L sequence is entirely compatible with the 'jelly-roll' beta-strand structure characteristic of the TNFs. Like the TNFs, CD40L is predicted to form a compact trimer, although the interactions between monomers are distinct from those found in the TNFs. The model predicts which regions of CD40L could interact with its receptor(s) and which amino acids are essential for the maintenance of its trimeric structure. | |||
A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors.,Peitsch MC, Jongeneel CV Int Immunol. 1993 Feb;5(2):233-8. PMID:8095800<ref>PMID:8095800</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1cda" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Jongeneel, C V]] | |||
[[Category: Peitsch, M C]] |
Latest revision as of 13:35, 14 July 2021
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A 3-DIMENSIONAL MODEL FOR THE CD40 LIGAND REVEALS A CLOSE SIMILARITY TO THE TUMOR NECROSIS FACTORSA 3-DIMENSIONAL MODEL FOR THE CD40 LIGAND REVEALS A CLOSE SIMILARITY TO THE TUMOR NECROSIS FACTORS
Structural highlights
Publication Abstract from PubMedBased on the similarity in primary structure between the newly characterized ligand for CD40 (CD40L) and the tumor necrosis factors (TNFs), we have modeled a detailed 3-D structure for CD40L. We used the known structure of TNF alpha as a template for the generation of the CD40L model. The soundness of the model-building algorithms was verified by constructing a 3-D model of TNF beta and comparing it to its crystallographically determined structure. The CD40L sequence is entirely compatible with the 'jelly-roll' beta-strand structure characteristic of the TNFs. Like the TNFs, CD40L is predicted to form a compact trimer, although the interactions between monomers are distinct from those found in the TNFs. The model predicts which regions of CD40L could interact with its receptor(s) and which amino acids are essential for the maintenance of its trimeric structure. A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors.,Peitsch MC, Jongeneel CV Int Immunol. 1993 Feb;5(2):233-8. PMID:8095800[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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