Domain structure of the mannose receptor (MR)

The mannose receptor (MR) can potentially internalize compounds that are recognized by three binding sites located in its extracellular region. It is subject to proteolytic processing and glycosylation, has a complex expression pattern and exhibits tissue-dependent binding properties. It is not surp...

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Bibliographic Details
Published inTrends in immunology Vol. 26; no. 2; p. 104
Main Authors Taylor, Philip R, Gordon, Siamon, Martinez-Pomares, Luisa
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Limited 01.02.2005
Subjects
Binding sites
Carbohydrates
Immune system
Lectins
Ligands
Pattern recognition
Proteins
Rodents
Surfactants
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ISSN1471-4906
1471-4981
DOI10.1016/j.it.2004.12.001

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Summary:The mannose receptor (MR) can potentially internalize compounds that are recognized by three binding sites located in its extracellular region. It is subject to proteolytic processing and glycosylation, has a complex expression pattern and exhibits tissue-dependent binding properties. It is not surprising, given this complexity, that the MR has been implicated in homeostatic processes, such as clearance of endogenous products and cell adhesion, as well as pathogen recognition and antigen presentation. In this Review, we summarize the current knowledge regarding the different aspects of MR binding properties, contribution to homeostatic clearance, cell activation and antigen presentation.
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ISSN:1471-4906
1471-4981
DOI:10.1016/j.it.2004.12.001