Multivariate model for Leaman score prediction including clinical features and retinal abnormalities.

<p>Multivariate model for Leaman score prediction including clinical features and retinal abnormalities.</p

Clinical features, retinal abnormalities and Leaman scores.

<p>Clinical features, retinal abnormalities and Leaman scores.</p

Multivariate model for Leaman score prediction including clinical features and retinal abnormalities.

<p>Multivariate model for Leaman score prediction including clinical features and retinal abnormalities.</p

Clinical features, retinal abnormalities and TIMI blush scores.

<p>Clinical features, retinal abnormalities and TIMI blush scores.</p

Arrangement of five overlapping collagen III α1 chains in the fibril D-period with overlap and gap zone indicated.

<p>Arrangement of five overlapping collagen III α1 chains in the fibril D-period with overlap and gap zone indicated.</p

The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.

Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I, with cell interaction domains, fibrillogenesis and enzyme cleavage domains, several major ligand-binding regions, and intermolecular crosslink sites at the same sites. These similarities allow heterotypic fibril formation with, and substitution by, collagen I in embryonic development and wound healing. The collagen III fibril assumes a "flexi-rod" structure with flexible zones interspersed with rod-like domains, which is consistent with the molecule's prominence in young, pliable tissues and distensible organs. Collagen III has two major hemostasis domains, with binding motifs for von Willebrand factor, α2β1 integrin, platelet binding octapeptide and glycoprotein VI, consistent with the bleeding tendency observed with COL3A1 disease-causing sequence variants

Missense mutation distribution in collagen III.

<p>Missense mutation frequency along the residues of the collagen III chain. This demonstrates the non-random distribution of variation.</p

Major structural features and ligand binding sites for collagen III.

<p>Major structural features and ligand binding sites for collagen III.</p

Arrangement of collagen I α1 (top), α2 (middle) and collagen III α1 (bottom) chains demonstrates approximate alignment of charge across all three molecules in the D-period.

<p>Arrangement of collagen I α1 (top), α2 (middle) and collagen III α1 (bottom) chains demonstrates approximate alignment of charge across all three molecules in the D-period.</p