Collagen amino acid sequence

Butler, W.T. (1970) Chemical Studies on the Cyanogen Bromide Peptides of Rat Skin Collagen. The Covalent Structure of al-CB5, the Major Hexose-containing Cyanogen Bromide Peptide of a V, Biochemistry, 9, 44-50 Butler, W.T., Finch, K.E. Miller, E.J. (1977) Covalent Structure of Cartilage Collagen. Amino Acid Sequence of Residues 363-551 of bovine al (II) Chains , Biochemistry, 16, 4981-90... 

Forsee, W.T., Springfield, J.D. Schutzbach, J.S. (1982) Effects of Phospholipids on al,2-Mannosidase Activity , Journal of Biological Chemistry, 257, 9963-7 Francis, G., Butler, W.T. Finch, J.E. (1978) The Covalent Structure of Cartilage Collagen. Amino Acid Sequence of Residues 552-661 of Bovine al (11) Chains , Biochemical Journal, 175, 921-30... 

Figure 14.1 Each polypeptide chain in the collagen molecule folds into an extended polyproline type II helix with a rise per turn along the helix of 9.6 A comprising 3.3 residues. In the collagen molecule three such chains are supercoiled about a common axis to form a 3000-A-long rod-like molecule. The amino acid sequence contains repeats of -Gly-X-Y- where X is often proline and Y is often hydroxyproline. (a) Ball and stick model of two turns of one polypeptide chain.

Fibrous proteins are long-chain polymers that are used as structural materials. Most contain specific repetitive amino acid sequences and fall into one of three groups coiled-coil a helices as in keratin and myosin triple helices as in collagen and p sheets as in silk and amyloid fibrils. 

The amino acid sequence of the collagen type I (bone, skin, tendon) is nearly completely known6. The sequence of the different tripeptides in the archain shows a more or less statistic distribution. The content of the tripeptides in the archain of type I collagen, however, is quite different (Table 1). 

Fig. 4. Helical structure of collagen, typical amino acid sequence within a collagen strand, and exchangeable versus non-exchangeable hydrogen atoms in an individual leucine molecule (Gly - glycine. Pro - Proline, Leu - leucine. Hyp - hydroxyproline.

Although the exact amino acid sequence differs between the various collagens, the primary structure usually conforms to a repeating tripeptide Gly-X-Y where X and Y are, proline, lysine, or hydroxyproline, hydroxylysine respectively. A single unit of collagen is a triple helix composed of three a chains. This conformation differs from the common a helix found in proteins in two important ways ... 

Nowadays, ACE inhibitory peptides have been isolated from meat, remaining muscle proteins, skin collagen and gelatin, bone, and internal organs of fishes such as Alaska pollack, bonito, tuna, salmon, shark, and sardine. Table 16.1 provides a partial summary of ACE inhibitory peptides derived from marine fish sources, their amino acid sequence, the enzyme used for hydrolysis, and IC50 values. The IC50 value is the concentration of peptide that inhibits 50% of ACE activity. 

Significant advances have been made in elucidating the primary structure of a-chains. The amino acid sequence of the ctj- and a2-chains of the helical region of collagen, residues 1—393 have been already reported192. ... 

Fietzek, P., Rexrodt, W. The covalent structure of collagen. The amino-acid sequence of a2-CH4 of calfskin collagen. Eur. J. Biochem. 59, 113 (1975)... 

The collagen superfamily of proteins includes more than twenty colla gen types, as well as additional proteins that have collagen-like domains. The three polypeptide a-chains are held together by hydro gen bonds between the chains. Variations in the amino acid sequence of the a-chains result in structural components that are about the same size (approximately 1000 amino acids long), but with slightly dif ferent properties. These a-chains are combined to form the various types of collagen found in the tissues. For example, the most common collagen, type I, contains two chains called a1 and one chain called... 

Amino acid sequence of a portion of the a1-chain of collagen. [Note Hyp is hydroxyproline and Hyl is hydroxylysine.]... 

Collagen has a most unusual amino acid composition in which glycine, proline, and hydroxyproline are the dominant amino acids. Further characterization of the polypeptide chains shows that these amino acids are arranged in a repetitious tripeptide sequence, Gly-X-Y, in which X is frequently a proline and Y is frequently a hydroxyproline. This unusual amino acid sequence and the unique diffraction pat-... 

In contrast, the X and Yresidues lie totally on the surface of the molecule, where they may interact readily with other molecules and hence specify the mode of molecular aggregation. The silk from the gooseberry sawfly Nematus ribesii gives a collagen-type X-ray diffraction pattern, which is strongly indicative that a triplet substructure also exists in its amino acid sequence. 

Fietzek, P. P., and Kuhn, K. (1975). Information contained in the amino acid sequence of the alphal(I)-chain of collagen and its consequences upon the formation of the triple helix, of fibrils and crosslinks. Mol. Cell. Biochem. 8, 141-157. 

Salem, G., and Traub, W. (1975). Conformational implications of amino acid sequence regularities in collagen. FEBS Lett. 51, 94—99. 

Delacoux, F., Fichard, A., Cogne, S., Garrone, R., and Ruggiero, F. (2000). Unraveling the amino acid sequence crucial for heparin binding to collagen V. J. Biol. Chem. 275, 29377-29382. 

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