1sz0: Difference between revisions

Revision as of 16:07, 21 February 2008

N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate

OverviewOverview

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 StructureAbout this Structure

1SZ0 is a Single protein structure of sequence from Bos taurus with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-[[Image:1sz0.gif|left|200px]]<br /><applet load="1sz0" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1sz0.gif|left|200px]]<br /><applet load="1sz0" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1sz0, resolution 2.10&Aring;" />
 '''N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate'''<br />
 ==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.
+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==
-SZ0 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SZ0 OCA].
+SZ0 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==
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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: M6P]]
 [[Category: NAG]]
@@ Line 21: / Line 21: @@
 [[Category: lectin; receptor; mannose 6-phosphate]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:51:41 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:07:44 2008''