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1281 12825 Ensembl ENSG00000168542 ENSMUSG00000026043 UniProt P02461 P08121 RefSeq (mRNA) NM_000090 NM_001376916 NM_009930 RefSeq (protein) NP_000081 NP_034060 Location (UCSC) Chr 2: 188.97 – 189.01 Mb Chr 1: 45.35 – 45.39 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Type III Collagen is a homotrimer, or a protein composed of three identical peptide chains (monomers), each ...
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The ratio and the proportion of collagen play an important role in the tensile and compressive strength, as well as the elasticity of the tissue. The content of collagen in cartilage is different between joints and soft tissue structures. [3] For example, cartilage in the knee has a different structure to the ankle. Cartilage, skin, and spinal ...
The most common form of collagen is fibrillary collagen. Another common form is meshwork collagen, which is often involved in the formation of filtration systems. All types of collagen are triple helices, but differ in the make-up of their alpha peptides created in step 2. Below we discuss the formation of fibrillary collagen.
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Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by homotrimers of collagen, type II, alpha 1 chains. It makes up 50% of all protein in cartilage and 85–90% of collagen of articular cartilage.
Type V collagen is a form of fibrillar [1] collagen associated with classical Ehlers-Danlos syndrome. It is found within the dermal/epidermal junction, placental tissues, as well as in association with tissues containing type I collagen. [2] Type V collagen is a part of the family of collagen proteins consisting of Collagen I- Collagen XXVIII.
FACIT collagen (Fibril Associated Collagens with Interrupted Triple helices [1]) is a type of collagen and also a proteoglycan [2] that have two or more triple-helical domains that connect to collagen fibrils and share protein domains with non-collagen matrix molecules. [3]