Sandbox GGC9

Crystal Structure of Collagen Adhesin and Collagen Complex

Collagen is one of the most abundance protein in the body. There are thought to be four types of collagen in which give rise to different structures of the body (bones, tendons, cartilage, skin, basement membranes, etc.) The collagenous domains have a characteristic triple helix structure where each of the participating polypeptides are repeating Gly-X-Y sequences that either form heterotrimeric or homotrimetric L-proline helices.[1] Both eukaryotic and prokayrotic express the collagen-binding protein such as ECM (Extracellular Matrix), celluar receptors, and bacterial adhesin.

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Function

Collagen composed three α-chains (procollagen)in which synthesize in the ER. Collagen is a strong, rope-like molecule, that can forms stretch resistant fibers. This fibrils are the most abundant protein in our bodies. There are 20 different types of collagen in our bodies each can adapt to the needs of specific tissue. Collagen are multifunctional glycoproteins that play an important role in cellular mophogenesis, cell signalling, tissue repairing, and cell migration in the human body. These protein are ubiquitously represent in tissues as part of the basement membrane (BM), in constitute a protective layer around the blood capillaries and are include in the extra cellular matrix (ECM). Which these tissues forms protective and structural such as bones, tendons, ligaments, cartilage, and skin. In both eukaryotic and prokaryotic, the binding of the collagen-binding protein happens in the A-domain.

Disease

Collagen-binding proteins(CBP) such as ECM (Extracellular Matrix) can be degrade via invasive pathogenic breach the basal lamina. Degradation of ECM can leads to major loss of mechanical containment molecules that protects the tissues from further pathogens. Furthermore, the pathogen will then degrade the interstitial space and connective tissues via ECM degrading proteases and/or the surface-bound plasminogen and matrix metalloprotein from the host. The adhesion of bacterial pathogen such as Staphylococcus aureus this particular adhesion calls "Collagen Hug".

Structural highlights

The collagen complex with binding protein represent in this view. Furthermore, this Ttriple helices represents the structure of procollagen (triple α-chain). The structural of hydroxyproline redisue of collagen. The particular amino acid residuess in the binding protein in this case CNA interact with the residue of the collagen base on the polarity and non-polar molecules.