1q25: Difference between revisions

Revision as of 15:35, 21 February 2008

Crystal structure of N-terminal 3 domains of CI-MPR

OverviewOverview

The 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR) mediates the intracellular transport of newly synthesized lysosomal enzymes containing mannose 6-phosphate on their N-linked oligosaccharides. In addition to its role in lysosome biogenesis, the CI-MPR interacts with a number of different extracellular ligands at the cell surface, including latent transforming growth factor-beta, insulin-like growth factor-II, plasminogen, and urokinase-type plasminogen activator receptor (uPAR), to regulate cell growth and motility. We have solved the crystal structure of the N-terminal 432 residues of the CI-MPR at 1.8 A resolution, which encompass three out of the 15 repetitive domains of its extracytoplasmic region. The three domains, which exhibit similar topology to each other and to the 46 kDa cation-dependent mannose 6-phosphate receptor, assemble into a compact structure with the uPAR/plasminogen and the carbohydrate-binding sites situated on opposite faces of the molecule. Knowledge of the arrangement of these three domains has allowed us to propose a model of the entire extracytoplasmic region of the CI-MPR that provides a context with which to envision the numerous binding interactions carried out by this multi-faceted receptor.

About this StructureAbout this Structure

1Q25 is a Single protein structure of sequence from Bos taurus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of uPAR, plasminogen, and sugar-binding sites of the 300 kDa mannose 6-phosphate receptor., Olson LJ, Yammani RD, Dahms NM, Kim JJ, EMBO J. 2004 May 19;23(10):2019-28. Epub 2004 Apr 15. PMID:15085180

Page seeded by OCA on Thu Feb 21 14:35:02 2008

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OCA

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-[[Image:1q25.gif|left|200px]]<br /><applet load="1q25" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1q25.gif|left|200px]]<br /><applet load="1q25" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1q25, resolution 1.80&Aring;" />
 '''Crystal structure of N-terminal 3 domains of CI-MPR'''<br />
 ==Overview==
-The 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), mediates the intracellular transport of newly synthesized lysosomal, enzymes containing mannose 6-phosphate on their N-linked oligosaccharides., In addition to its role in lysosome biogenesis, the CI-MPR interacts with, a number of different extracellular ligands at the cell surface, including, latent transforming growth factor-beta, insulin-like growth factor-II, plasminogen, and urokinase-type plasminogen activator receptor (uPAR), to, regulate cell growth and motility. We have solved the crystal structure of, the N-terminal 432 residues of the CI-MPR at 1.8 A resolution, which, encompass three out of the 15 repetitive domains of its extracytoplasmic, region. The three domains, which exhibit similar topology to each other, and to the 46 kDa cation-dependent mannose 6-phosphate receptor, assemble, into a compact structure with the uPAR/plasminogen and the, carbohydrate-binding sites situated on opposite faces of the molecule., Knowledge of the arrangement of these three domains has allowed us to, propose a model of the entire extracytoplasmic region of the CI-MPR that, provides a context with which to envision the numerous binding, interactions carried out by this multi-faceted receptor.
+The 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR) mediates the intracellular transport of newly synthesized lysosomal enzymes containing mannose 6-phosphate on their N-linked oligosaccharides. In addition to its role in lysosome biogenesis, the CI-MPR interacts with a number of different extracellular ligands at the cell surface, including latent transforming growth factor-beta, insulin-like growth factor-II, plasminogen, and urokinase-type plasminogen activator receptor (uPAR), to regulate cell growth and motility. We have solved the crystal structure of the N-terminal 432 residues of the CI-MPR at 1.8 A resolution, which encompass three out of the 15 repetitive domains of its extracytoplasmic region. The three domains, which exhibit similar topology to each other and to the 46 kDa cation-dependent mannose 6-phosphate receptor, assemble into a compact structure with the uPAR/plasminogen and the carbohydrate-binding sites situated on opposite faces of the molecule. Knowledge of the arrangement of these three domains has allowed us to propose a model of the entire extracytoplasmic region of the CI-MPR that provides a context with which to envision the numerous binding interactions carried out by this multi-faceted receptor.
 ==About this Structure==
-Q25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q25 OCA].
+Q25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q25 OCA].
 ==Reference==
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 [[Category: Bos taurus]]
 [[Category: Single protein]]
-[[Category: Dahms, N.M.]]
+[[Category: Dahms, N M.]]
-[[Category: Kim, J.J.P.]]
+[[Category: Kim, J J.P.]]
-[[Category: Olson, L.J.]]
+[[Category: Olson, L J.]]
 [[Category: GOL]]
 [[Category: mannose 6-phosphate]]
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 [[Category: receptor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:19:12 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:02 2008''