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Hydroxyproline is a major component of the protein collagen, [3] comprising roughly 13.5% of mammalian collagen. Hydroxyproline and proline play key roles for collagen stability. [4] They permit the sharp twisting of the collagen helix. [5]
Two tyrosines separated by a single amino acid, typically valine or another tyrosine, form a short intra-molecular diphenylether crosslink. [11] This can be crosslinked further by the enzyme extensin peroxidase [12] [13] [14] to form an inter-molecular bridge between extensin molecules and thus form networks and sheets.
They are members of the wider class of hydroxyproline (Hyp)-rich cell wall glycoproteins, a large and diverse group of glycosylated wall proteins. AGPs have been reported in a wide range of higher plants in seeds, roots, stems, leaves and inflorescences. AGPs account for only a small portion of the cell wall, usually no more than 1% of dry mass ...
Glycoproteins vary greatly in composition, making many different compounds such as antibodies or hormones. [4] Due to the wide array of functions within the body, interest in glycoprotein synthesis for medical use has increased. [5] There are now several methods to synthesize glycoproteins, including recombination and glycosylation of proteins. [5]
In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. [2] [3] Collagen folded into a triple helix is known as tropocollagen.
Additionally, structural proteins (1-5%) are found in most plant cell walls; they are classified as hydroxyproline-rich glycoproteins (HRGP), arabinogalactan proteins (AGP), glycine-rich proteins (GRPs), and proline-rich proteins (PRPs). Each class of glycoprotein is defined by a characteristic, highly repetitive protein sequence.
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HRG is a glycoprotein of 70-75kDa present at a relatively high concentration in the plasma of vertebrates.The primary structure of human HRG is predicted to be a 507 amino acid multidomain polypeptide consisting of two cystatin-like regions at the N-terminus, a histidine-rich region (HRR) flanked by proline-rich regions (PRR), and a C-terminal domain. [10]