Evidence map›Paper›PMID 17656581›Full record

ArticleProtein science : a publication of the Protein Society2007

The structure of receptor-associated protein (RAP).

Donghan Lee, Joseph D Walsh, Molly Migliorini, Ping Yu, Tao Cai, Charles D Schwieters, Susan Krueger, Dudley K Strickland, Yun-Xing Wang

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 25% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 23 citations in OpenAlex.

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  14. Activated protein C ligation of ApoER2 (LRP8) causes Dab1-dependent signaling in U937 cells.Proceedings of the National Academy of Sciences of the United States of America · 2009
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 6 institutions in 1 country.

Donghan LeeProtein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, National Cancer Institute at Frederick, National Institutes of Health, Frederick, Maryland 21702, USA.
Joseph D Walsh
Molly Migliorini
Ping Yu
Tao Cai
Charles D Schwieters
Susan Krueger
Dudley K Strickland
Yun-Xing Wang
National Institutes of Health · USScience Applications International Corporation (United States) · USCenter for Information Technology · USFrederick National Laboratory for Cancer Research · USNIST Center for Neutron Research · USUniversity of Maryland, Baltimore · US

Funding

tPA and LRP in StrokeP01HL054710 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI STRICKLAND, DUDLEY K. · 1996 to 2011
$17.3M
Regulation of Surface Receptors by LRPR01HL050784 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI STRICKLAND, DUDLEY K. · 1993 to 2011
$3.8M
STRUCTURE OF BIOMACROMOLECULAR FUNCTION &ACTIVITYZ01BC010379 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WANG, YUN XING M · 2000 to 2008
$2.0M
Intramural NIH HHSNCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400NCI NIH HHS N01-CO56000NHLBI NIH HHS HL50784NHLBI NIH HHS HL54710NHLBI NIH HHS P01 HL054710NHLBI NIH HHS R01 HL050784
6 · The paper itself

Abstract

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.

Indexed as

Binding SitesLDL-Receptor Related Protein-Associated ProteinModels, MolecularNeutron DiffractionNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein Structure, TertiaryScattering, Small AngleLDL-Receptor Related Protein-Associated Protein

Identifiers

PMID17656581
PMCPMC2203372
OpenAlexW1990264554

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.