Source:http://linkedlifedata.com/resource/pubmed/id/15213425
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2004-6-23
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| pubmed:abstractText |
The 39 kDa receptor-associated protein (RAP) is an endoplasmic reticulum resident protein that binds tightly to the low-density lipoprotein receptor-related protein (LRP) as well as to other members of the low-density lipoprotein receptor superfamily. The association of RAP with LRP prevents this receptor from interacting with ligands. RAP is a three-domain protein that contains two independent LRP binding sites; one located within domains 1 and 2, and one located within domain 3. As the first step toward defining the structure of the full-length protein and understanding the interaction between RAP and this family of receptors, we have determined the 3D structure of domain 1 using constraints derived from heteronuclear multi-dimensional NMR spectra, including NOEs, dihedral angles, J-couplings and chemical shifts, as well as two sets of non-correlated residual dipolar couplings measured from the protein solutions in anisotropic media of Pf1 and 6% polyacrylamide gel. The backbone C(alpha) rmsd between the current structure and a homo-nuclear NOE-based structure is about 2 A. The large rmsd mainly reflects the significant differences in helical orientation and in the structural details of the long helix (helix 2) between the two structures.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acrylic Resins,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon,
http://linkedlifedata.com/resource/pubmed/chemical/LDL-Receptor Related Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protons,
http://linkedlifedata.com/resource/pubmed/chemical/polyacrylamide
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0925-2738
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
29
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
271-9
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:15213425-Acrylic Resins,
pubmed-meshheading:15213425-Anisotropy,
pubmed-meshheading:15213425-Binding Sites,
pubmed-meshheading:15213425-Carbon,
pubmed-meshheading:15213425-Databases as Topic,
pubmed-meshheading:15213425-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:15213425-Endoplasmic Reticulum,
pubmed-meshheading:15213425-Humans,
pubmed-meshheading:15213425-Hydrogen Bonding,
pubmed-meshheading:15213425-LDL-Receptor Related Proteins,
pubmed-meshheading:15213425-Ligands,
pubmed-meshheading:15213425-Magnetic Resonance Spectroscopy,
pubmed-meshheading:15213425-Models, Molecular,
pubmed-meshheading:15213425-Protein Conformation,
pubmed-meshheading:15213425-Protein Structure, Tertiary,
pubmed-meshheading:15213425-Proteins,
pubmed-meshheading:15213425-Protons,
pubmed-meshheading:15213425-Software
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| pubmed:year |
2004
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| pubmed:articleTitle |
NMR structural studies of domain 1 of receptor-associated protein.
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| pubmed:affiliation |
Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, National Cancer Institute at Frederick, National Institutes of Health, Frederick, MD 21702, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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