Linked Life Data

14516194

Source:http://linkedlifedata.com/resource/pubmed/id/14516194

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
2003-9-30
pubmed:abstractText
Procollagen VII is a homotrimer of 350-kDa proalpha1(VII) chains. Each chain has a central collagenous domain flanked by a noncollagenous amino-terminal NC1 domain and a carboxy-terminal NC2 domain. After secretion from cells, procollagen VII molecules form antiparallel dimers with a 60 nm overlap. These dimers are stabilized by disulfide bonds formed between cysteines present in the NC2 domain and cysteines present in the triple-helical domain. Electron microscopy has provided direct evidence for the existence of collagen VII dimers, but the dynamic process of dimer formation is not well understood. In the present study, we tested the hypothesis that, during dimer formation, the NC2 domain of one procollagen VII molecule specifically recognizes and binds to the triple-helical region adjacent to Cys-2625 of another procollagen VII molecule. We also investigated the role of processing of the NC2 domain by the procollagen C-proteinase/BMP-1 in dimer assembly. We engineered mini mouse procollagen VII variants consisting of intact NC1 and NC2 domains and a shortened triple helix in which the C-terminal region encompassing Cys-2625 was either preserved or substituted with the region encompassing Cys-1448 derived from the N-terminal part of the triple-helical domain. The results indicate that procollagen VII self-assembly depends on site-specific interactions between the NC2 domain and the triple-helical region adjacent to Cys-2625 and that this process is promoted by the cleavage of the NC2 by procollagen C-proteinase/BMP1.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11434-42
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:14516194-Amino Acid Sequence, pubmed-meshheading:14516194-Animals, pubmed-meshheading:14516194-Binding Sites, pubmed-meshheading:14516194-Biotin, pubmed-meshheading:14516194-Bone Morphogenetic Protein 1, pubmed-meshheading:14516194-Bone Morphogenetic Proteins, pubmed-meshheading:14516194-Cloning, Molecular, pubmed-meshheading:14516194-Collagen Type VII, pubmed-meshheading:14516194-Colorimetry, pubmed-meshheading:14516194-Cysteine, pubmed-meshheading:14516194-Dimerization, pubmed-meshheading:14516194-Disulfides, pubmed-meshheading:14516194-Humans, pubmed-meshheading:14516194-Metalloendopeptidases, pubmed-meshheading:14516194-Mice, pubmed-meshheading:14516194-Microscopy, Electron, pubmed-meshheading:14516194-Models, Molecular, pubmed-meshheading:14516194-Molecular Sequence Data, pubmed-meshheading:14516194-Protein Binding, pubmed-meshheading:14516194-Protein Structure, Secondary, pubmed-meshheading:14516194-Protein Structure, Tertiary, pubmed-meshheading:14516194-Recombinant Proteins, pubmed-meshheading:14516194-Sequence Deletion
pubmed:year
2003
pubmed:articleTitle
Procollagen VII self-assembly depends on site-specific interactions and is promoted by cleavage of the NC2 domain with procollagen C-proteinase.
pubmed:affiliation
Department of Dermatology and Cutaneous Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.