answer

Most collagen forms in a similar manner🚨but the following process is typical for type I:

with loss of teeth; skin discolors

Vitamin C deficiency causes scurvy🚨a serious and painful disease in which defective collagen prevents the formation of strong connective tissue. Gums deteriorate and bleed

An autoimmune disease such as lupus erythematosus or rheumatoid arthritis[34] may attack healthy collagen fibers.🚨

which destroys collagen or interferes with its production.

Many bacteria and viruses secrete virulence factors🚨such as the enzyme collagenase

is used to make up larger collagen aggregates

A single collagen molecule🚨tropocollagen

this means approximately half of the collagen sequence is not glycine

A distinctive feature of collagen is the regular arrangement of amino acids in each of the three chains of these collagen subunits. The sequence often follows the pattern Gly-Pro-X or Gly-X-Hyp🚨where X may be any of various other amino acid residues.[29] Proline or hydroxyproline constitute about 1/6 of the total sequence. With glycine accounting for the 1/3 of the sequence

tissue regulation

Collagen is not only a structural protein. Due to its key role in the determination of cell phenotype🚨cell adhesion

Gly is required at every third position because the assembly of the triple helix puts this residue at the interior (axis) of the helix

Because glycine is the smallest amino acid with no side chain🚨it plays a unique role in fibrous structural proteins. In collagen

into even larger arrays in the extracellular spaces of tissues.[35][36] Additional assembly of fibrils is guided by fibroblasts

The tropocollagen subunits spontaneously self-assemble🚨with regularly staggered ends

glycoproteins

There is some covalent crosslinking within the triple helices🚨and a variable amount of covalent crosslinking between tropocollagen helices forming well organized aggregates (such as fibrils).[39] Larger fibrillar bundles are formed with the aid of several different classes of proteins (including different collagen types)

staggered array. 40?nm gaps between the ends of the tropocollagen subunits (approximately equal to the gap region) probably serve as nucleation sites for the deposition of long

Collagen fibrils/aggregates are arranged in different combinations and concentrations in various tissues to provide varying tissue properties. In bone🚨entire collagen triple helices lie in a parallel

postranslational modification

Collagen-related diseases most commonly arise from genetic defects or nutritional deficiencies that affect the biosynthesis🚨assembly

In addition to the above-mentioned disorders🚨excessive deposition of collagen occurs in scleroderma.

One thousand mutations have been identified in 12 out of more than 20 types of collagen. These mutations can lead to various diseases at the tissue level.[46]🚨

results in weak bones and irregular connective tissue

Osteogenesis imperfecta ÿ Caused by a mutation in type 1 collagen🚨dominant autosomal disorder

Chondrodysplasias ÿ Skeletal disorder believed to be caused by a mutation in type 2 collagen🚨further research is being conducted to confirm this.[48]

are known. Some types can be lethal

Ehlers-Danlos syndrome ÿ Six different types of this disorder🚨which lead to deformities in connective tissue

but also as both an autosomal dominant and autosomal recessive disorder

Alport syndrome ÿ Can be passed on genetically🚨usually as X-linked dominant

associated with reduced levels of collagen in the skin and bones

Osteoporosis ÿ Not inherited genetically🚨brought on with age

Knobloch syndrome ÿ Caused by a mutation in the COL18A1 gene that codes for the production of collagen XVIII. Patients present with protrusion of the brain tissue and degeneration of the retina; an individual who has family members suffering from the disorder is at an increased risk of developing it themselves since there is a hereditary link.[46]🚨