1m6p: Difference between revisions

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New page: left|200px<br /><applet load="1m6p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m6p, resolution 1.8Å" /> '''EXTRACYTOPLASMIC DOMA...
 
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[[Image:1m6p.jpg|left|200px]]<br /><applet load="1m6p" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1m6p.jpg|left|200px]]<br /><applet load="1m6p" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1m6p, resolution 1.8&Aring;" />
caption="1m6p, resolution 1.8&Aring;" />
'''EXTRACYTOPLASMIC DOMAIN OF BOVINE CATION-DEPENDENT MANNOSE 6-PHOSPHATE RECEPTOR'''<br />
'''EXTRACYTOPLASMIC DOMAIN OF BOVINE CATION-DEPENDENT MANNOSE 6-PHOSPHATE RECEPTOR'''<br />


==Overview==
==Overview==
Targeting of newly synthesized lysosomal hydrolases to the lysosome is, mediated by the cation-dependent mannose 6-phosphate receptor (CD-MPR) and, the insulin-like growth factor II/cation-independent mannose 6-phosphate, receptor (IGF-II/CI-MPR). The two receptors, which share sequence, similarities, constitute the P-type family of animal lectins. We now, report the three-dimensional structure of a glycosylation-deficient, yet, fully functional form of the extracytoplasmic domain of the bovine CD-MPR, (residues 3-154) complexed with mannose 6-phosphate at 1.8 A resolution., The extracytoplasmic domain of the CD-MPR crystallizes as a dimer, and, each monomer folds into a nine-stranded flattened beta barrel, which bears, a striking resemblance to avidin. The distance of 40 A between the two, ligand-binding sites of the dimer provides a structural basis for the, observed differences in binding affinity exhibited by the CD-MPR toward, various lysosomal enzymes.
Targeting of newly synthesized lysosomal hydrolases to the lysosome is mediated by the cation-dependent mannose 6-phosphate receptor (CD-MPR) and the insulin-like growth factor II/cation-independent mannose 6-phosphate receptor (IGF-II/CI-MPR). The two receptors, which share sequence similarities, constitute the P-type family of animal lectins. We now report the three-dimensional structure of a glycosylation-deficient, yet fully functional form of the extracytoplasmic domain of the bovine CD-MPR (residues 3-154) complexed with mannose 6-phosphate at 1.8 A resolution. The extracytoplasmic domain of the CD-MPR crystallizes as a dimer, and each monomer folds into a nine-stranded flattened beta barrel, which bears a striking resemblance to avidin. The distance of 40 A between the two ligand-binding sites of the dimer provides a structural basis for the observed differences in binding affinity exhibited by the CD-MPR toward various lysosomal enzymes.


==About this Structure==
==About this Structure==
1M6P 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 MN and M6P as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M6P OCA].  
1M6P 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=MN:'>MN</scene> and <scene name='pdbligand=M6P:'>M6P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M6P OCA].  


==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Dahms, N.M.]]
[[Category: Dahms, N M.]]
[[Category: Kim, J.J.P.]]
[[Category: Kim, J J.P.]]
[[Category: Roberts, D.L.]]
[[Category: Roberts, D L.]]
[[Category: Weix, D.J.]]
[[Category: Weix, D J.]]
[[Category: M6P]]
[[Category: M6P]]
[[Category: MN]]
[[Category: MN]]
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[[Category: transport]]
[[Category: transport]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:11:18 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:08 2008''

Revision as of 14:52, 21 February 2008

File:1m6p.jpg


1m6p, resolution 1.8Å

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EXTRACYTOPLASMIC DOMAIN OF BOVINE CATION-DEPENDENT MANNOSE 6-PHOSPHATE RECEPTOR

OverviewOverview

Targeting of newly synthesized lysosomal hydrolases to the lysosome is mediated by the cation-dependent mannose 6-phosphate receptor (CD-MPR) and the insulin-like growth factor II/cation-independent mannose 6-phosphate receptor (IGF-II/CI-MPR). The two receptors, which share sequence similarities, constitute the P-type family of animal lectins. We now report the three-dimensional structure of a glycosylation-deficient, yet fully functional form of the extracytoplasmic domain of the bovine CD-MPR (residues 3-154) complexed with mannose 6-phosphate at 1.8 A resolution. The extracytoplasmic domain of the CD-MPR crystallizes as a dimer, and each monomer folds into a nine-stranded flattened beta barrel, which bears a striking resemblance to avidin. The distance of 40 A between the two ligand-binding sites of the dimer provides a structural basis for the observed differences in binding affinity exhibited by the CD-MPR toward various lysosomal enzymes.

About this StructureAbout this Structure

1M6P is a Single protein structure of sequence from Bos taurus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Molecular basis of lysosomal enzyme recognition: three-dimensional structure of the cation-dependent mannose 6-phosphate receptor., Roberts DL, Weix DJ, Dahms NM, Kim JJ, Cell. 1998 May 15;93(4):639-48. PMID:9604938

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