2i83: Difference between revisions
New page: left|200px<br /> <applet load="2i83" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i83" /> '''hyaluronan-binding domain of CD44 in its li... |
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[[Image:2i83.gif|left|200px]]<br /> | [[Image:2i83.gif|left|200px]]<br /><applet load="2i83" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''hyaluronan-binding domain of CD44 in its ligand-bound form'''<br /> | '''hyaluronan-binding domain of CD44 in its ligand-bound form'''<br /> | ||
==Overview== | ==Overview== | ||
CD44, a major cell surface receptor for hyaluronan (HA), contains a | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
2I83 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2I83 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Sakakura, M.]] | [[Category: Sakakura, M.]] | ||
[[Category: Shimada, I.]] | [[Category: Shimada, I.]] | ||
[[Category: Sugahara, K | [[Category: Sugahara, K N.]] | ||
[[Category: Takeda, M.]] | [[Category: Takeda, M.]] | ||
[[Category: Terasawa, H.]] | [[Category: Terasawa, H.]] | ||
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[[Category: link module]] | [[Category: link module]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:50:06 2008'' | ||
Revision as of 15:50, 21 February 2008
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hyaluronan-binding domain of CD44 in its ligand-bound form
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
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