Evidence map›Paper›PMID 19276170›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2009

The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding.

Kemin Tan, Mark Duquette, Andrzej Joachimiak, Jack Lawler

Abstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

39 citing papers in PubMed, 75 citations in OpenAlex.

  1. Phylogenetic Analysis and Structural Evaluation ofbioRxiv : the preprint server for biology · 2026
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  18. Cartilage oligomeric matrix protein: COMPopathies and beyond.Matrix biology : journal of the International Society for Matrix Biology · 2018
    Review
  19. Two novel mutations ofHuman genome variation · 2018
    Article
  20. Article
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

4 authors at 4 institutions in 2 countries.

Kemin TanMidwest Center for Structural Genomics, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, USA.
Mark Duquette
Andrzej Joachimiak
Jack Lawler
Argonne National Laboratory · USBeth Israel Deaconess Medical Center · USHadassah Medical Center · ILJoint Center for Structural Genomics · US

Funding

THROMBOSPONIN-4R01HL049081 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI LAWLER, JOHN W · 1994 to 2010
$3.8M
NHLBI NIH HHS HL49081NHLBI NIH HHS R01 HL049081
6 · The paper itself

Abstract

Cartilage oligomeric matrix protein (COMP), or thrombospondin-5 (TSP-5), is a secreted glycoprotein that is important for growth plate organization and function. Mutations in COMP cause two skeletal dysplasias, pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (EDM1). In this study, we determined the structure of a recombinant protein that contains the last epidermal growth factor repeat, the type 3 repeats and the C-terminal domain (CTD) of COMP to 3.15-A resolution limit by X-ray crystallography. The CTD is a beta-sandwich that is composed of 15 antiparallel beta-strands, and the type 3 repeats are a contiguous series of calcium binding sites that associate with the CTD at multiple points. The crystal packing reveals an exposed potential metal-ion-dependent adhesion site (MIDAS) on one edge of the beta-sandwich that is common to all TSPs and may serve as a binding site for collagens and other ligands. Disease-causing mutations in COMP disrupt calcium binding, disulfide bond formation, intramolecular interactions, or sites for potential ligand binding. The structure presented here and its unique molecular packing in the crystal identify potential interactive sites for glycosaminoglycans, integrins, and collagens, which are key to cartilage structure and function.

Indexed as

Base SequenceBinding SitesCartilage Oligomeric Matrix ProteinCollagenCrystallography, X-RayCysteineDNA, ComplementaryExtracellular Matrix ProteinsGlycoproteinsGlycosaminoglycansHumansIntegrinsIn Vitro TechniquesLigandsMatrilin ProteinsModels, Moleculararginyl-glycyl-aspartic acidCartilage Oligomeric Matrix ProteinCollagenCysteineDNA, ComplementaryExtracellular Matrix ProteinsGlycoproteinsGlycosaminoglycansIntegrinsLigandsMatrilin ProteinsOligopeptidesRecombinant ProteinsThrombospondin 1Thrombospondin 2ThrombospondinsTSP5 protein, human

Identifiers

PMID19276170
PMCPMC2717772
OpenAlexW2131587303

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.