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| {{STRUCTURE_1uuh| PDB=1uuh | SCENE= }} | | {{STRUCTURE_1uuh| PDB=1uuh | SCENE= }} |
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| '''HYALURONAN BINDING DOMAIN OF HUMAN CD44'''
| | ===HYALURONAN BINDING DOMAIN OF HUMAN CD44=== |
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| ==Overview==
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| Adhesive interactions involving CD44, the cell surface receptor for hyaluronan, underlie fundamental processes such as inflammatory leukocyte homing and tumor metastasis. Regulation of such events is critical and appears to be effected by changes in CD44 N-glycosylation that switch the receptor "on" or "off" under appropriate circumstances. How altered glycosylation influences binding of hyaluronan to the lectin-like Link module in CD44 is unclear, although evidence suggests additional flanking sequences peculiar to CD44 may be involved. Here we show using X-ray crystallography and NMR spectroscopy that these sequences form a lobular extension to the Link module, creating an enlarged HA binding domain and a formerly unidentified protein fold. Moreover, the disposition of key N-glycosylation sites reveals how specific sugar chains could alter both the affinity and avidity of CD44 HA binding. Our results provide the necessary structural framework for understanding the diverse functions of CD44 and developing novel therapeutic strategies.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14992719}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14992719 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14992719}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Receptor]] | | [[Category: Receptor]] |
| [[Category: Sugar-binding]] | | [[Category: Sugar-binding]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:42:34 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:34:12 2008'' |
