2fyj: Difference between revisions

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[[Image:2fyj.~~gif~~|left|200px]]

[[Image:2fyj.png|left|200px]]

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~~'''~~NMR Solution structure of calcium-loaded LRP double module~~'''~~

===NMR Solution structure of calcium-loaded LRP double module===

~~==Overview==~~

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~~The low~~-~~density lipoprotein receptor~~-~~related protein (LRP) interacts with more than 30 ligands of different sizes and structures that can all be replaced by the receptor-associated protein (RAP).~~ The ~~double module of complement type repeats~~, ~~CR56~~, ~~of LRP binds many ligands including all three domains of RAP and alpha2-macroglobulin, which promotes~~ the ~~catabolism of~~ the ~~Abeta-peptide implicated in Alzheimer's disease~~. ~~To understand the receptor-ligand cross-talk, the NMR structure of CR56 has been solved and ligand binding experiments with RAP domain 1 (RAPd1~~) ~~have been performed. From chemical shift perturbations of both binding partners upon complex formation~~, ~~a HADDOCK model of~~ the ~~complex between CR56 and RAPd1 has been obtained~~. ~~The binding residues are similar to a common binding motif suggested from alpha2~~-~~macroglobulin binding studies and provide evidence for an understanding of their mutual cross~~-competition pattern. The present structural results convey a simultaneous description of both binding partners of an LRP-ligand complex and open a route to a broader understanding of the binding specificity of the LRP receptor, which may involve a general four-residue receptor-ligand recognition motif common to all LRP ligands. The present result may be beneficial in the design of antagonists of ligand binding to the LDL receptor family, and especially of drugs for treatment of Alzheimer's disease.

The line below this paragraph, {{ABSTRACT_PUBMED_16938309}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16938309 is the PubMed ID number.

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==About this Structure==

2FYJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYJ OCA].

2FYJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYJ OCA].

==Reference==

Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif., Jensen GA, Andersen OM, Bonvin AM, Bjerrum-Bohr I, Etzerodt M, Thogersen HC, O'Shea C, Poulsen FM, Kragelund BB, J Mol Biol. 2006 Sep 29;362(4):700-16. Epub 2006 Jul 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16938309 16938309]

The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein., Nielsen PR, Ellgaard L, Etzerodt M, Thogersen HC, Poulsen FM, Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7521-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9207124 9207124]

Identification of the minimal functional unit in the low density lipoprotein receptor-related protein for binding the receptor-associated protein (RAP). A conserved acidic residue in the complement-type repeats is important for recognition of RAP., Andersen OM, Christensen LL, Christensen PA, Sorensen ES, Jacobsen C, Moestrup SK, Etzerodt M, Thogersen HC, J Biol Chem. 2000 Jul 14;275(28):21017-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10747921 10747921]

[[Category: Homo sapiens]]

[[Category: Single protein]]

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[[Category: Double module]]

[[Category: Loop-structure]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 04~~:27:12 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:40:19 2008''

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-[[Image:2fyj.gif|left|200px]]
+{{Seed}}
+[[Image:2fyj.png|left|200px]]
 <!--
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 {{STRUCTURE_2fyj|  PDB=2fyj  |  SCENE=  }}
-'''NMR Solution structure of calcium-loaded LRP double module'''
+===NMR Solution structure of calcium-loaded LRP double module===
-==Overview==
+<!--
-The low-density lipoprotein receptor-related protein (LRP) interacts with more than 30 ligands of different sizes and structures that can all be replaced by the receptor-associated protein (RAP). The double module of complement type repeats, CR56, of LRP binds many ligands including all three domains of RAP and alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease. To understand the receptor-ligand cross-talk, the NMR structure of CR56 has been solved and ligand binding experiments with RAP domain 1 (RAPd1) have been performed. From chemical shift perturbations of both binding partners upon complex formation, a HADDOCK model of the complex between CR56 and RAPd1 has been obtained. The binding residues are similar to a common binding motif suggested from alpha2-macroglobulin binding studies and provide evidence for an understanding of their mutual cross-competition pattern. The present structural results convey a simultaneous description of both binding partners of an LRP-ligand complex and open a route to a broader understanding of the binding specificity of the LRP receptor, which may involve a general four-residue receptor-ligand recognition motif common to all LRP ligands. The present result may be beneficial in the design of antagonists of ligand binding to the LDL receptor family, and especially of drugs for treatment of Alzheimer's disease.
+The line below this paragraph, {{ABSTRACT_PUBMED_16938309}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16938309 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16938309}}
 ==About this Structure==
-FYJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYJ OCA].
+FYJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYJ OCA].
 ==Reference==
 Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif., Jensen GA, Andersen OM, Bonvin AM, Bjerrum-Bohr I, Etzerodt M, Thogersen HC, O'Shea C, Poulsen FM, Kragelund BB, J Mol Biol. 2006 Sep 29;362(4):700-16. Epub 2006 Jul 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16938309 16938309]
+The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein., Nielsen PR, Ellgaard L, Etzerodt M, Thogersen HC, Poulsen FM, Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7521-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9207124 9207124]
+Identification of the minimal functional unit in the low density lipoprotein receptor-related protein for binding the receptor-associated protein (RAP). A conserved acidic residue in the complement-type repeats is important for recognition of RAP., Andersen OM, Christensen LL, Christensen PA, Sorensen ES, Jacobsen C, Moestrup SK, Etzerodt M, Thogersen HC, J Biol Chem. 2000 Jul 14;275(28):21017-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10747921 10747921]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
@@ Line 35: / Line 43: @@
 [[Category: Double module]]
 [[Category: Loop-structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:27:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:40:19 2008''