Recent progress on collagen triple helix structure, stability and assembly.
Collagen is the major structural protein in skin, bone, tendon, cartilage and blood vessels. Its triple helical structure has been long studied by fibre diffraction. More recently, single crystal X-ray diffraction on collagen-like polypeptide models has allowed a significantly improved description of the triple helix and it has shed light on the relationships between triple helix features and stability. This review outlines the current knowledge regarding collagen triple helix structure, stability, and assembly, with a particular emphasis on the latest structural results.
Centro di Studio di Biocristallografia, CNR, Via Mezzocannone 6, I-80134 Napoli, Italy.
Rita
R
Berisio
Luigi
L
Vitagliano
Lelio
L
Mazzarella
Adriana
A
Zagari
D000818:Animals; D003094:Collagen / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D013696:Temperature
D010455:Peptides; D003094:Collagen