![]() ![]() A significant advance was achieved when, in the same 1951 issue of the Proceedings of the National Academy of Sciences in which he and coworkers put forth the correct structures for the α-helix and β-sheet, Pauling & Corey ( 12) proposed a structure for collagen. In 1940, Astbury & Bell ( 11) proposed that the collagen molecule consists of a single extended polypeptide chain with all amide bonds in the cis conformation. In animals, individual collagen triple helices, known as tropocollagen (TC), assemble in a complex, hierarchical manner that ultimately leads to the macroscopic fibers and networks observed in tissue, bone, and basement membranes ( Figure 2). ProHypGly is the most common triplet (10.5%) in collagen ( 9). The amino acids in the Xaa and Yaa positions of collagen are often (2 S)-proline (Pro, 28%) and (2 S,4 R)-4-hydroxyproline (Hyp, 38%), respectively. This repeat occurs in all types of collagen, although it is disrupted at certain locations within the triple-helical domain of nonfibrillar collagens ( 8). The tight packing of PPII helices within the triple helix mandates that every third residue be Gly, resulting in a repeating XaaYaaGly sequence, where Xaa and Yaa can be any amino acid. The defining feature of collagen is an elegant structural motif in which three parallel polypeptide strands in a left-handed, polyproline II-type (PPII) helical conformation coil about each other with a one-residue stagger to form a right-handed triple helix ( Figure 1). That discovery is, however, under challenge ( 5, 6). Remarkably, intact collagen has been discovered in soft tissue of the fossilized bones of a 68 million-year-old Tyrannosaurus rex fossil ( 3, 4), by far the oldest protein detected to date. Twenty-eight different types of collagen composed of at least 46 distinct polypeptide chains have been identified in vertebrates, and many other proteins contain collagenous domains ( 1, 2). ![]() In humans, collagen comprises one-third of the total protein, accounts for three-quarters of the dry weight of skin, and is the most prevalent component of the extracellular matrix (ECM). Collagen is an abundant structural protein in all animals. ![]()
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