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1m6p
From Proteopedia
(New page: 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=" | + | [[Image:1m6p.jpg|left|200px]]<br /><applet load="1m6p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m6p, resolution 1.8Å" /> | caption="1m6p, resolution 1.8Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: Dahms, N M.]] |
| - | [[Category: Kim, J | + | [[Category: Kim, J J.P.]] |
| - | [[Category: Roberts, D | + | [[Category: Roberts, D L.]] |
| - | [[Category: Weix, D | + | [[Category: Weix, D J.]] |
[[Category: M6P]] | [[Category: M6P]] | ||
[[Category: MN]] | [[Category: MN]] | ||
| Line 24: | Line 24: | ||
[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:08 2008'' |
Revision as of 11:52, 21 February 2008
|
EXTRACYTOPLASMIC DOMAIN OF BOVINE CATION-DEPENDENT MANNOSE 6-PHOSPHATE RECEPTOR
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.
About this Structure
1M6P is a Single protein structure of sequence from Bos taurus with and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:52:08 2008
