2i83
From Proteopedia
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hyaluronan-binding domain of CD44 in its ligand-bound form
Contents |
Overview
CD44, a major cell surface receptor for hyaluronan (HA), contains a functional domain responsible for HA binding at its N terminus (residues 21-178). Accumulating evidence indicates that proteolytic cleavage of CD44 in its extracellular region (residues 21-268) leads to enhanced tumor cell migration and invasion. Hence, understanding the mechanisms underlying the CD44 proteolytic cleavage is important for understanding the mechanism of CD44-mediated tumor progression. Here we present the NMR structure of the HA-binding domain of CD44 in its HA-bound state. The structure is composed of the Link module (residues 32-124) and an extended lobe (residues 21-31 and 125-152). Interestingly, a comparison of its unbound and HA-bound structures revealed that rearrangement of the beta-strands in the extended lobe (residues 143-148) and disorder of the structure in the following C-terminal region (residues 153-169) occurred upon HA binding, which is consistent with the results of trypsin proteolysis studies of the CD44 HA-binding domain. The order-to-disorder transition of the C-terminal region by HA binding may be involved in the CD44-mediated cell migration.
Disease
Known diseases associated with this structure: Blood group, Indian system OMIM:[107269], Fertile eunuch syndrome OMIM:[138850], Hypogonadotropic hypogonadism OMIM:[138850]
About this Structure
2I83 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Ligand-induced structural changes of the CD44 hyaluronan-binding domain revealed by NMR., Takeda M, Ogino S, Umemoto R, Sakakura M, Kajiwara M, Sugahara KN, Hayasaka H, Miyasaka M, Terasawa H, Shimada I, J Biol Chem. 2006 Dec 29;281(52):40089-95. Epub 2006 Nov 2. PMID:17085435
Page seeded by OCA on Thu Mar 20 17:26:32 2008
