2fyl: Difference between revisions

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[[Image:2fyl.gif|left|200px]]<br />

[[Image:2fyl.gif|left|200px]]<br /><applet load="2fyl" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2fyl" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2fyl" />

'''Haddock model of the complex between double module of LRP, CR56, and first domain of receptor associated protein, RAP-d1.'''<br />

==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 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.

==Disease==

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==About this Structure==

2FYL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2FYL OCA].

2FYL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYL OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Protein complex]]

[[Category: Andersen, O.M.]]

[[Category: Andersen, O M.]]

[[Category: Bjerrum-Bohr, I.]]

[[Category: Bonvin, A.M.]]

[[Category: Bonvin, A M.]]

[[Category: Etzerodt, M.]]

[[Category: Jensen, G.A.]]

[[Category: Jensen, G A.]]

[[Category: Kragelund, B.B.]]

[[Category: Kragelund, B B.]]

[[Category: Poulsen, F.M.]]

[[Category: Poulsen, F M.]]

[[Category: shea, C.O.]]

[[Category: shea, C O.]]

[[Category: CA]]

[[Category: complex]]

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[[Category: shift-mapping]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 22~~:12:~~07 2007~~''

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@@ Line 1: / Line 1: @@
-[[Image:2fyl.gif|left|200px]]<br />
+[[Image:2fyl.gif|left|200px]]<br /><applet load="2fyl" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2fyl" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2fyl" />
 '''Haddock model of the complex between double module of LRP, CR56, and first domain of receptor associated protein, RAP-d1.'''<br />
 ==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 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.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-FYL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FYL OCA].
+FYL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYL OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Andersen, O.M.]]
+[[Category: Andersen, O M.]]
 [[Category: Bjerrum-Bohr, I.]]
-[[Category: Bonvin, A.M.]]
+[[Category: Bonvin, A M.]]
 [[Category: Etzerodt, M.]]
-[[Category: Jensen, G.A.]]
+[[Category: Jensen, G A.]]
-[[Category: Kragelund, B.B.]]
+[[Category: Kragelund, B B.]]
-[[Category: Poulsen, F.M.]]
+[[Category: Poulsen, F M.]]
-[[Category: shea, C.O.]]
+[[Category: shea, C O.]]
 [[Category: CA]]
 [[Category: complex]]
@@ Line 32: / Line 31: @@
 [[Category: shift-mapping]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:12:07 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:26:28 2008''