1lre
From Proteopedia
(New page: 200px<br /> <applet load="1lre" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lre" /> '''RECEPTOR ASSOCIATED PROTEIN (RAP) DOMAIN 1,...) |
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| - | [[Image:1lre.gif|left|200px]]<br /> | + | [[Image:1lre.gif|left|200px]]<br /><applet load="1lre" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1lre" size=" | + | |
caption="1lre" /> | caption="1lre" /> | ||
'''RECEPTOR ASSOCIATED PROTEIN (RAP) DOMAIN 1, NMR, 20 STRUCTURES'''<br /> | '''RECEPTOR ASSOCIATED PROTEIN (RAP) DOMAIN 1, NMR, 20 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the N-terminal domain (residues 18-112) | + | The three-dimensional structure of the N-terminal domain (residues 18-112) of alpha2-macroglobulin receptor-associated protein (RAP) has been determined by NMR spectroscopy. The structure consists of three helices composed of residues 23-34, 39-65, and 73-88. The three helices are arranged in an up-down-up antiparallel topology. The C-terminal 20 residues were shown not to be in a well defined conformation. A structural model for the binding of RAP to the family of low-density lipoprotein receptors is proposed. It defines a role in binding for both the unordered C terminus and the structural scaffold of the core structure. Pathogenic epitopes for the rat disease Heymann nephritis, an experimental model of human membranous glomerulonephritis, have been identified in RAP and in the large endocytic receptor gp330/megalin. Here we provide the three-dimensional structure of the pathogenic epitope in RAP. The amino acid residues known to form the epitope are in a helix-loop-helix conformation, and from the structure it is possible to rationalize the published results obtained from studies of fragments of the N-terminal domain. |
==About this Structure== | ==About this Structure== | ||
| - | 1LRE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1LRE is a [http://en.wikipedia.org/wiki/Single_protein 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=1LRE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Nielsen, P | + | [[Category: Nielsen, P R.]] |
| - | [[Category: Poulsen, F | + | [[Category: Poulsen, F M.]] |
[[Category: alpha2-macroglobulin receptor associated protein]] | [[Category: alpha2-macroglobulin receptor associated protein]] | ||
[[Category: helix bundle]] | [[Category: helix bundle]] | ||
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[[Category: low density lipoprotein receptor family associated protein]] | [[Category: low density lipoprotein receptor family associated protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:39 2008'' |
Revision as of 11:47, 21 February 2008
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RECEPTOR ASSOCIATED PROTEIN (RAP) DOMAIN 1, NMR, 20 STRUCTURES
Overview
The three-dimensional structure of the N-terminal domain (residues 18-112) of alpha2-macroglobulin receptor-associated protein (RAP) has been determined by NMR spectroscopy. The structure consists of three helices composed of residues 23-34, 39-65, and 73-88. The three helices are arranged in an up-down-up antiparallel topology. The C-terminal 20 residues were shown not to be in a well defined conformation. A structural model for the binding of RAP to the family of low-density lipoprotein receptors is proposed. It defines a role in binding for both the unordered C terminus and the structural scaffold of the core structure. Pathogenic epitopes for the rat disease Heymann nephritis, an experimental model of human membranous glomerulonephritis, have been identified in RAP and in the large endocytic receptor gp330/megalin. Here we provide the three-dimensional structure of the pathogenic epitope in RAP. The amino acid residues known to form the epitope are in a helix-loop-helix conformation, and from the structure it is possible to rationalize the published results obtained from studies of fragments of the N-terminal domain.
About this Structure
1LRE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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:9207124
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