Collagen II containing a Cys substitution for arg-alpha1-519. Homotrimeric monomers containing the mutation do not assemble into fibrils but alter the self-assembly of the normal protein.
Publication/Presentation Date
3-7-1997
Abstract
A recombinant system was used to prepare human type II procollagen containing the substitution of Cys for Arg at alpha1-519 found in three unrelated families with early onset generalized osteoarthritis together with features of a mild chondrodysplasia probably best classified as spondyloepiphyseal dysplasia. In contrast to mutated procollagens containing Cys substitutions for obligatory Gly residues, the Cys substitution at alpha1-519 did not generate any intramolecular disulfide bonds. The results were consistent with computer modeling experiments that demonstrated that the alpha carbon distances were shorter with Cys substitutions for obligatory Gly residues than with Cys substitutions in the Y position residues in repeating -Gly-X-Y- sequences of the collagen triple helix. The mutated collagen did not assemble into fibrils under conditions in which the normal monomers polymerized. However, the presence of the mutated monomer in mixtures with normal collagen II increased the lag time for fibril assembly and altered the morphology of the fibrils formed.
Volume
272
Issue
10
First Page
6457
Last Page
6464
ISSN
0021-9258
Published In/Presented At
Fertala, A., Ala-Kokko, L., Wiaderkiewicz, R., & Prockop, D. J. (1997). Collagen II containing a Cys substitution for arg-alpha1-519. Homotrimeric monomers containing the mutation do not assemble into fibrils but alter the self-assembly of the normal protein. The Journal of biological chemistry, 272(10), 6457–6464. https://doi.org/10.1074/jbc.272.10.6457
Disciplines
Medicine and Health Sciences
PubMedID
9045670
Department(s)
Department of Pathology and Laboratory Medicine
Document Type
Article