1CGD

HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE

Summary for 1CGD

Entry DOI	10.2210/pdb1cgd/pdb
Descriptor	COLLAGEN-LIKE PEPTIDE, ACETIC ACID (3 entities in total)
Functional Keywords	collagen, collagen hydration, hydroxyproline, connective tissue, extracellular matrix
Total number of polymer chains	3
Total formula weight	8534.93
Authors	Bella, J.,Brodsky, B.,Berman, H.M. (deposition date: 1995-06-09, release date: 1996-06-20, Last modification date: 2018-04-18)
Primary citation	Bella, J.,Brodsky, B.,Berman, H.M. Hydration structure of a collagen peptide. Structure, 3:893-906, 1995 Cited by PubMed Abstract: The collagen triple helix is a unique protein motif defined by the supercoiling of three polypeptide chains in a polyproline II conformation. It is a major domain of all collagen proteins and is also reported to exist in proteins with host defense function and in several membrane proteins. The triple-helical domain has distinctive properties. Collagen requires a high proportion of the post-translationally modified imino acid 4-hydroxyproline and water to stabilize its conformation and assembly. The crystal structure of a collagen-like peptide determined to 1.85 Angstrum showed that these two features may be related. PubMed: 8535783 DOI: 10.1016/S0969-2126(01)00224-6 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.85 Å)

Structure validation