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1sz0
From Proteopedia
(New page: 200px<br /><applet load="1sz0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sz0, resolution 2.10Å" /> '''N-terminal 3 domains...) |
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| - | [[Image:1sz0.gif|left|200px]]<br /><applet load="1sz0" size=" | + | [[Image:1sz0.gif|left|200px]]<br /><applet load="1sz0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sz0, resolution 2.10Å" /> | caption="1sz0, resolution 2.10Å" /> | ||
'''N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate'''<br /> | '''N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 300-kDa cation-independent mannose 6-phosphate receptor (CI-MPR) plays | + | The 300-kDa cation-independent mannose 6-phosphate receptor (CI-MPR) plays a critical role in the trafficking of newly synthesized mannose 6-phosphate-containing acid hydrolases to the lysosome. The receptor contains two high affinity carbohydrate recognition sites within its 15-domain extracytoplasmic region, with essential residues for carbohydrate recognition located in domain 3 and domain 9. Previous studies have shown that these two sites are distinct with respect to carbohydrate specificity. In addition, expression of truncated forms of the CI-MPR demonstrated that domain 9 can be expressed as an isolated domain, retaining high affinity (Kd approximately 1 nm) carbohydrate binding, whereas expression of domain 3 alone resulted in a protein capable of only low affinity binding (Kd approximately 1 microm) toward a lysosomal enzyme. In the current report the crystal structure of the N-terminal 432 residues of the CI-MPR, encompassing domains 1-3, was solved in the presence of bound mannose 6-phosphate. The structure reveals the unique architecture of this carbohydrate binding pocket and provides insight into the ability of this site to recognize a variety of mannose-containing sugars. |
==About this Structure== | ==About this Structure== | ||
| - | 1SZ0 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 NAG, OS and M6P as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1SZ0 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=NAG:'>NAG</scene>, <scene name='pdbligand=OS:'>OS</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=1SZ0 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: Olson, L | + | [[Category: Olson, L J.]] |
[[Category: M6P]] | [[Category: M6P]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
| Line 21: | Line 21: | ||
[[Category: lectin; receptor; mannose 6-phosphate]] | [[Category: lectin; receptor; mannose 6-phosphate]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:07:44 2008'' |
Revision as of 13:07, 21 February 2008
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N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate
Overview
The 300-kDa cation-independent mannose 6-phosphate receptor (CI-MPR) plays a critical role in the trafficking of newly synthesized mannose 6-phosphate-containing acid hydrolases to the lysosome. The receptor contains two high affinity carbohydrate recognition sites within its 15-domain extracytoplasmic region, with essential residues for carbohydrate recognition located in domain 3 and domain 9. Previous studies have shown that these two sites are distinct with respect to carbohydrate specificity. In addition, expression of truncated forms of the CI-MPR demonstrated that domain 9 can be expressed as an isolated domain, retaining high affinity (Kd approximately 1 nm) carbohydrate binding, whereas expression of domain 3 alone resulted in a protein capable of only low affinity binding (Kd approximately 1 microm) toward a lysosomal enzyme. In the current report the crystal structure of the N-terminal 432 residues of the CI-MPR, encompassing domains 1-3, was solved in the presence of bound mannose 6-phosphate. The structure reveals the unique architecture of this carbohydrate binding pocket and provides insight into the ability of this site to recognize a variety of mannose-containing sugars.
About this Structure
1SZ0 is a Single protein structure of sequence from Bos taurus with , and as ligands. Full crystallographic information is available from OCA.
Reference
The N-terminal carbohydrate recognition site of the cation-independent mannose 6-phosphate receptor., Olson LJ, Dahms NM, Kim JJ, J Biol Chem. 2004 Aug 6;279(32):34000-9. Epub 2004 May 28. PMID:15169779
Page seeded by OCA on Thu Feb 21 15:07:44 2008
