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2i83
From Proteopedia
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| - | [[Image:2i83.gif|left|200px]] | + | [[Image:2i83.gif|left|200px]] |
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| - | '''hyaluronan-binding domain of CD44 in its ligand-bound form''' | + | {{Structure |
| + | |PDB= 2i83 |SIZE=350|CAPTION= <scene name='initialview01'>2i83</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''hyaluronan-binding domain of CD44 in its ligand-bound form''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2I83 is a [ | + | 2I83 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I83 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17085435 17085435] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: link module]] | [[Category: link module]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:26:32 2008'' |
Revision as of 15:26, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
