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Molecular organization, structural features, and ligand binding characteristics of CD44, a highly variable cell surface glycoprotein with multiple functions
Author(s) -
Bajorath Jürgen
Publication year - 2000
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(20000501)39:2<103::aid-prot1>3.0.co;2-g
Subject(s) - cd44 , gene isoform , microbiology and biotechnology , extracellular matrix , cell surface receptor , ligand (biochemistry) , signal transduction , biology , transmembrane protein , cell , receptor , computational biology , chemistry , biochemistry , gene
CD44 is a type I transmembrane protein and member of the cartilage link protein family. It is involved in cell‐cell and cell‐matrix interactions and signal transduction. Several CD44 ligands have been identified. CD44 is a major cell surface receptor for hyaluronan, a component of the extracellular matrix. It is implicated in diseases such as cancer and inflammation and therefore intensely studied. A characteristic feature of CD44 is the occurrence of many isoforms that are expressed in a cell‐specific manner and differentially glycosylated. Although a number of CD44 isoforms have been characterized, the structural diversity of CD44 makes it often challenging to study (isoform‐specific) CD44‐ligand interactions at the molecular level of detail. The structural organization and ligand binding characteristics of CD44 are focal points of this review. On the basis of recent structural and mutagenesis studies, details of the CD44‐hyaluronan interaction are beginning to be understood. Proteins 2000;39:103–111. © 2000 Wiley‐Liss, Inc.

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