Sandbox GGC9: Difference between revisions
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==Crystal Structure of Collagen Adhesin and Collagen Complex== | ==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. | 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. | ||
<Structure load='2f6a' size='350' frame='true' align='right' caption='Insert caption here' scene='Collagenadhesincomplex/1' /> | <Structure load='2f6a' size='350' frame='true' align='right' caption='Insert caption here' scene='Collagenadhesincomplex/1' /> | ||
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== Disease == | == 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 adhesin of bac | |||
== Structural highlights == | == Structural highlights == | ||
Revision as of 03:03, 23 April 2018
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
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 adhesin of bac
Structural highlights
This is the structural resiude of 4-HydroxyprolineCollagen Adhesion and Complex by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
