2p03
From Proteopedia
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| - | [[Image:2p03.jpg|left|200px]] | + | [[Image:2p03.jpg|left|200px]] |
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| - | '''The structure of receptor-associated protein(RAP)''' | + | {{Structure |
| + | |PDB= 2p03 |SIZE=350|CAPTION= <scene name='initialview01'>2p03</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= LRPAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''The structure of receptor-associated protein(RAP)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2P03 is a [ | + | 2P03 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=2P03 OCA]. |
==Reference== | ==Reference== | ||
| - | The structure of receptor-associated protein (RAP)., Lee D, Walsh JD, Migliorini M, Yu P, Cai T, Schwieters CD, Krueger S, Strickland DK, Wang YX, Protein Sci. 2007 Aug;16(8):1628-40. PMID:[http:// | + | The structure of receptor-associated protein (RAP)., Lee D, Walsh JD, Migliorini M, Yu P, Cai T, Schwieters CD, Krueger S, Strickland DK, Wang YX, Protein Sci. 2007 Aug;16(8):1628-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17656581 17656581] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: receptor-associated protein]] | [[Category: receptor-associated protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:06:48 2008'' |
Revision as of 16:06, 20 March 2008
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| Gene: | LRPAP1 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The structure of receptor-associated protein(RAP)
Overview
The receptor-associated protein (RAP) is a molecular chaperone that binds tightly to certain newly synthesized LDL receptor family members in the endoplasmic reticulum (ER) and facilitates their delivery to the Golgi. We have adopted a divide-and-conquer strategy to solve the structures of the individual domains of RAP using NMR spectroscopy. We present here the newly determined structure of domain 2. Based on this structure and the structures of domains 1 and 3, which were solved previously, we utilized experimental small-angle neutron scattering (SANS) data and a novel simulated annealing protocol to characterize the overall structure of RAP. The results reveal that RAP adopts a unique structural architecture consisting of three independent three-helix bundles that are connected by long and flexible linkers. The flexible linkers and the quasi-repetitive structural architecture may allow RAP to adopt various possible conformations when interacting with the LDL receptors, which are also made of repetitive substructure units.
About this Structure
2P03 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of receptor-associated protein (RAP)., Lee D, Walsh JD, Migliorini M, Yu P, Cai T, Schwieters CD, Krueger S, Strickland DK, Wang YX, Protein Sci. 2007 Aug;16(8):1628-40. PMID:17656581
Page seeded by OCA on Thu Mar 20 18:06:48 2008
