1kjb: Difference between revisions
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[[ | ==THEORETICAL MODEL OF L-SELECTIN, C-TYPE LECTIN DOMAIN, RESIDUES 1-120, CELL ADHESION MOLECULE== | ||
<StructureSection load='1kjb' size='340' side='right'caption='[[1kjb]]' 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=1KJB 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=1kjb FirstGlance], [https://www.ebi.ac.uk/pdbsum/1kjb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kjb ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We have complemented multiple sequence alignments of the lectin domains of the selectins with an analysis of structurally invariant regions in X-ray structures of the mannose-binding protein (MBP) and E-selectin. The analysis shows that regions of structural conservation between MBP and E-selectin extend beyond regions of rigorous sequence conservation within the selectin family and suggests that reliable three-dimensional models of selectins from different species can be generated by modification of only a few backbone segments in E-selectin. A model of the L-selectin lectin domain is built and discussed with regard to observed differences in selectin specificity. | |||
A template for generation and comparison of three-dimensional selectin models.,Bajorath J, Aruffo A Biochem Biophys Res Commun. 1995 Nov 22;216(3):1018-23. PMID:7488174<ref>PMID:7488174</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1kjb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Aruffo, A]] | [[Category: Aruffo, A]] | ||
[[Category: Bajorath, J]] | [[Category: Bajorath, J]] | ||
Latest revision as of 09:54, 11 August 2021
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THEORETICAL MODEL OF L-SELECTIN, C-TYPE LECTIN DOMAIN, RESIDUES 1-120, CELL ADHESION MOLECULETHEORETICAL MODEL OF L-SELECTIN, C-TYPE LECTIN DOMAIN, RESIDUES 1-120, CELL ADHESION MOLECULE
Structural highlights
Publication Abstract from PubMedWe have complemented multiple sequence alignments of the lectin domains of the selectins with an analysis of structurally invariant regions in X-ray structures of the mannose-binding protein (MBP) and E-selectin. The analysis shows that regions of structural conservation between MBP and E-selectin extend beyond regions of rigorous sequence conservation within the selectin family and suggests that reliable three-dimensional models of selectins from different species can be generated by modification of only a few backbone segments in E-selectin. A model of the L-selectin lectin domain is built and discussed with regard to observed differences in selectin specificity. A template for generation and comparison of three-dimensional selectin models.,Bajorath J, Aruffo A Biochem Biophys Res Commun. 1995 Nov 22;216(3):1018-23. PMID:7488174[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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