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Your Most Plentiful Protein

COLLAGEN Your Most Plentiful Protein About one quarter of all of the protein in your

About one quarter of all of the protein in your body is collagen. Collagen is a major structural protein, forming molecular cables that strengthen the tendons and vast, resilient sheets that support the skin and internal organs. Bones and teeth are made by adding mineral crystals to collagen. Collagen provides structure to our bodies, protecting and supporting the softer tissues and connecting them with the skeleton. But, in spite of its critical function in the body, collagen is a relatively simple protein.

About the RCSB PDB Molecule of the Month

Using selected molecules from the PDB archive, each feature includes an introduction to the structure and function of the molecule, a discussion of its relevance to human health and welfare, and suggestions for viewing and accessing further details.

and suggestions for viewing and accessing further details. The RCSB PDB Molecule of the Month is

The RCSB PDB Molecule of the Month is read by students, teachers, and scientists worldwide at

This April 2000 edition was written and illustrated by David S. Goodsell (RCSB PDB and The Scripps Research Institute).

The Collagen Triple Helix

Collagen is composed of three chains, wound together in a tight triple helix. The illustration included here shows only a small segment of the entire molecule–each chain is over 1400 amino acids long and only about 20 are shown here. A repeated sequence of three amino acids forms this sturdy structure. Every third amino acid is glycine, a small amino acid that fits perfectly inside the helix. Many of the remaining posi- tions in the chain are filled by two unexpected amino acids: proline and a modified version of proline, hydroxyproline. We wouldn't expect proline to be this common, because it forms a kink in the polypeptide chain that is difficult to accommodate in typical globular proteins. But, as you can see on the next page, it seems to be just the right shape for this structural protein.

Vitamin C

Hydroxyproline, which is critical for collagen stability, is created by modifying normal proline amino acids after the collagen chain is built. The reaction requires vitamin C to assist in the addi- tion of oxygen. Unfortunately, we cannot make

vitamin C within our bodies, and if we don't get enough in our diet, the results can be disastrous. Vitamin C deficiency slows the production of hydroxyproline and stops the construction of new collagen, ultimately causing scurvy. The symptoms of scurvy–loss of teeth and easy bruis- ing–are caused by the lack of collagen to repair the wear-and-tear caused by everyday activities.

Collagen on the Grocery Shelf

Collagen from livestock animals is a familiar ingredient for cooking. Like most proteins, when collagen is heated, it loses all of its struc- ture. The triple helix unwinds and the chains separate. Then, when this denatured mass of tan- gled chains cools down, it soaks up all of the sur- rounding water like a sponge, forming gelatin.

Ropes and Ladders

We make many different kinds of collagen, which form long ropes and tough sheets that are used for structural support in mature animals and as pathways for cellular movement during development. All contain a long stretch of triple helix connected to different types of ends. The simplest is merely a long triple helix, with blunt

RCSB Protein Data Bank The Protein Data Bank (PDB) is the single worldwide repository for

RCSB Protein Data Bank

The Protein Data Bank (PDB) is the single worldwide repository for the processing and distribution of 3D structure data of large molecules of proteins and nucleic acids. The RCSB PDB is operated by Rutgers, The State University of New Jersey and the San Diego Supercomputer Center and the Skaggs School of Pharmacy and Pharmaceutical Sciences at the University of California, San Diego–two members of the Research Collaboratory for Structural Bioinformatics (RCSB).

It is supported by funds from the National Science Foundation, the National Institute of General Medical Sciences, the Office of Science, Department of Energy, the National Library of Medicine, the National Cancer Institute, the National Institute of Neurological Disorders and Stroke and the National Institute of Diabetes & Digestive & Kidney Diseases.

The RCSB PDB is a member of the worldwide PDB (wwPDB;

is a member of the worldwide PDB ( wwPDB; ). References: 1cag: J. Bella, M.


1cag: J. Bella, M. Eaton, B. Brodsky, H. M. Berman (1994) Crystal and molecular structure of a collagen- like peptide at 1.9 A resolution. Science 266: 75-81

1bkv: R. Z. Kramer, J. Bella, P. Mayville, B. Brodsky, H. M. Berman (1999) Sequence dependent conforma- tional variations of collagen triple-helical structure. Nat.Struct.Biol. 6: 454-457


structure. Nat.Struct.Biol. 6 : 454-457 COLLAGEN ends. These "type I" collagen molecules associate

ends. These "type I" collagen molecules associate side-by-side, like fibers in a rope, to form tough fib- rils. These fibrils crisscross the space between nearly every one of our cells. The illustration above depicts a basement mem- brane, which forms a tough surface that supports the skin and many organs. A different collagen– "type IV"–forms the structural basis of this mem- brane. Type IV collagen has a globular head at one end and an extra tail at the other. The heads bind strongly together, head-to-head, and four collagen molecules associate together through their tails, forming an X-shaped complex. Using these two types of interactions, type IV collagen forms an extended network, shown here in light blue. Two other molecules–cross-shaped laminin (blue- green) and long, snaky proteoglycans (green)–fill in the spaces, forming a dense sheet.

Exploring the Structure


A special amino acid sequence makes the tight colla- gen triple helix particularly stable. Every third amino acid is a glycine, and many of the remaining amino acids are proline or hydroxyproline. A classic triple helix is shown here, and may be viewed in the PDB file 1cag. Notice how the glycine forms a tiny elbow packed inside the helix, and notice how the proline and hydroxyproline smoothly bend the chain back around the helix. In this structure, the researchers placed a larger alanine amino acid in the position nor- mally occupied by glycine, showing that it crowds the neighboring chains.


This collagen helix contains a segment of human collagen, and may be viewed in the PDB file 1bkv. Notice that the top half is very uniform, where the sequence is the ideal mixture of glycine and pro- lines. At the bottom, the helix is less regular, because many different amino acids are placed between the equally-spaced glycines.