From Tumor Necrosis Factor Receptor to RANK, from the Selectins and Link Proteins to CD44: New Molecular Models of Cell Surface Receptors and Analysis of Specificity Determinants |
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Authors: | Jürgen Bajorath |
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Institution: | (1) MDS Panlabs, Computational Chemistry & Informatics, 11804 North Creek Pkwy. S., Bothell, WA, 98011-8805, USA. Tel (425) 487-8297, Fax (425) 487-8262. E-mail: jbajorath@panlabs.com, US;(2) Department of Biological Structure, University of Washington, Seattle, Washington 98195, USA., US |
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Abstract: | Modeling and structure-function studies on two cell surface proteins are presented, which are implicated in the regulation of immune responses and cell adhesion. In the first part, model building of RANK, a new member of the tumor necrosis factor receptor (TNFR) superfamily (TNFRSF), is reported. The model is analyzed in light of structural studies on the TNFR-ligand complex and molecular model-based mutagenesis analyses of CD40-ligand and Fas-ligand interactions. The study makes it possible to predict residues important for ligand binding to RANK and further rationalizes differences in specificity between TNFR-like cell surface receptors. In the second part, recent investigations on the structure and carbohydrate binding site of CD44, a member of the link protein family, are discussed. The binding site in CD44 is compared to calcium-dependent (C-type) lectins, which include the selectins, another family of cell adhesion molecules. The studies on TNFRSF members and link proteins reported herein complement a recent review article in this journal, which focused on modeling and binding site analysis of immune cell surface proteins.Electronic Supplementary Material available. |
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Keywords: | Cell surface proteins" target="_blank">gif" alt="ensp" align="MIDDLE" BORDER="0"> Cell surface proteins protein superfamilies molecular models binding sites specificity |
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