Work

The tissue form of type VII collagen is an antiparallel dimer.

Year: 1986

Type: article

Abstract: We recently reported the partial characterization of a new human collagen termed Type VII. This molecule is distinctive among the collagen family in that it contains three identical subunit alpha chains within a triple helical domain 424 nm in length. The molecule contains three identical alpha chains which are genetically distinct from other known collagens. Previous studies indicate that a portion of the limited pepsin-solubilized molecules appears to exist as antiparallel dimers associated by disulfide bonds. In this report, we demonstrate that the major tissue form of Type VII collagen is a dimer, associated by disulfide bonds through a 60-nm overlap of the aminoterminal triple helical ends. Intermolecular disulfide bonds occur only within this overlap region. Interchain disulfide bonds exist in the carboxyl terminal 7% of the molecule and may exist within the overlap region as well. Disulfide bond-stabilized aggregates larger than dimers are not seen.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(19)57262-3

Authors: N P Morris, D R Keene, R W Glanville, H Bentz, R E Burgeson

Language: English

Topic: Collagen: Extraction and Characterization

Subfield: Biomaterials

Field: Materials Science

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funder: National Institutes of Health

Award: CHARACTERIZATION OF A NEW HUMAN COLLAGEN