1esl
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(New page: 200px<br /> <applet load="1esl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1esl, resolution 2.0Å" /> '''INSIGHT INTO E-SELEC...)
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Revision as of 14:39, 12 November 2007
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INSIGHT INTO E-SELECTIN(SLASH)LIGAND INTERACTION FROM THE CRYSTAL STRUCTURE AND MUTAGENESIS OF THE LEC(SLASH)EGF DOMAINS
Contents |
Overview
The three-dimensional structure of the ligand-binding region of human, E-selectin has been determined at 2.0 A resolution. The structure reveals, limited contact between the two domains and a coordination of Ca2+ not, predicted from other C-type lectins. Structure/function analysis indicates, a defined region and specific amino-acid side chains that may be involved, in ligand binding. These features of the E-selectin/ligand interaction, have important implications for understanding the recruitment of, leukocytes to sites of inflammation.
Disease
Known diseases associated with this structure: Atherosclerosis, susceptibility to OMIM:[131210], Blood pressure regulation QTL OMIM:[131210], IgA nephropathy, susceptiblity to OMIM:[131210]
About this Structure
1ESL is a Single protein structure of sequence from Homo sapiens with CA and CL as ligands. Full crystallographic information is available from OCA.
Reference
Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains., Graves BJ, Crowther RL, Chandran C, Rumberger JM, Li S, Huang KS, Presky DH, Familletti PC, Wolitzky BA, Burns DK, Nature. 1994 Feb 10;367(6463):532-8. PMID:7509040
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