Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-4-28
pubmed:abstractText
The N-terminal fragment of rat cartilage oligomeric matrix protein (COMP), comprising residues 20-83, was over-expressed in E. coli and purified under non-denaturing conditions. The fragment forms pentamers similar to the assembly domain of the native protein. Its five chains can be covalently linked in vitro by oxidation of cysteines 68 and 71. The fragment adopts a predominantly alpha-helical structure as judged by circular dichroism spectroscopy. On the basis of these findings we propose the model of a five-stranded alpha-helical bundle for the assembly domain of COMP. The studied sequence is conserved in thrombospondins 3 and 4 thus raising the possibility that these proteins are also pentamers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
341
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
54-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8137922-Amino Acid Sequence, pubmed-meshheading:8137922-Animals, pubmed-meshheading:8137922-Base Sequence, pubmed-meshheading:8137922-Cartilage, pubmed-meshheading:8137922-Circular Dichroism, pubmed-meshheading:8137922-Cloning, Molecular, pubmed-meshheading:8137922-DNA, pubmed-meshheading:8137922-Disulfides, pubmed-meshheading:8137922-Escherichia coli, pubmed-meshheading:8137922-Extracellular Matrix Proteins, pubmed-meshheading:8137922-Glycoproteins, pubmed-meshheading:8137922-Humans, pubmed-meshheading:8137922-Membrane Proteins, pubmed-meshheading:8137922-Microscopy, Electron, pubmed-meshheading:8137922-Molecular Sequence Data, pubmed-meshheading:8137922-Protein Structure, Secondary, pubmed-meshheading:8137922-Rats, pubmed-meshheading:8137922-Recombinant Proteins, pubmed-meshheading:8137922-Sequence Homology, Amino Acid, pubmed-meshheading:8137922-Thrombospondins
pubmed:year
1994
pubmed:articleTitle
The thrombospondin-like chains of cartilage oligomeric matrix protein are assembled by a five-stranded alpha-helical bundle between residues 20 and 83.
pubmed:affiliation
Department of Biophysical Chemistry, Biozentrum University, Basel, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't