Linked Life Data

12064927

Source:http://linkedlifedata.com/resource/pubmed/id/12064927

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2002-6-14
pubmed:abstractText
Fibril-forming collagens are synthesized in precursor form, procollagens, with N- and C-terminal propeptide extensions. The C-propeptides direct chain association during intracellular assembly of the procollagen molecule from its three constituent polypeptide chains. Following or during secretion into the extracellular matrix, propeptides are cleaved by specific procollagen proteinases, thereby triggering fibril formation. The recent determination of the low-resolution structure of the C-propeptide trimer gives insights into the mechanism of procollagen chain association. In the extracellular matrix, the procollagen C-propeptides ensure procollagen solubility, while persistence of the N-propeptides controls fibril shape. Mechanisms for the control of fibril diameter are reviewed in terms of the radial packing model for collagen fibril structure. Finally, procollagen molecules have recently been shown to undergo liquid crystalline ordering in solution, prior to fibril assembly. This may provide an explanation for the liquid crystal-like suprafibrillar architectures of different connective tissues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1047-8477
pubmed:author
pubmed:copyrightInfo
(c) 2002 Elsevier Science (USA).
pubmed:issnType
Print
pubmed:volume
137
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2-10
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Building collagen molecules, fibrils, and suprafibrillar structures.
pubmed:affiliation
Institut de Biologie et Chimie des Protéines, CNRS UMR 5086, Lyon, France.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't