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Your Most Plentiful Protein

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.

The Collagen Triple Helix vitamin C within our bodies, and if we don't get
enough in our diet, the results can be disastrous.
Collagen is composed of three chains, wound
Vitamin C deficiency slows the production of
together in a tight triple helix. The illustration
hydroxyproline and stops the construction of
included here shows only a small segment of the
new collagen, ultimately causing scurvy. The
entire molecule–each chain is over 1400 amino
symptoms of scurvy–loss of teeth and easy bruis-
acids long and only about 20 are shown here. A
ing–are caused by the lack of collagen to repair the
repeated sequence of three amino acids forms
wear-and-tear caused by everyday activities.
this sturdy structure. Every third amino acid is
glycine, a small amino acid that fits perfectly Collagen on the Grocery Shelf
inside the helix. Many of the remaining posi-
Collagen from livestock animals is a familiar
tions in the chain are filled by two unexpected
ingredient for cooking. Like most proteins,
amino acids: proline and a modified version of
when collagen is heated, it loses all of its struc-
proline, hydroxyproline. We wouldn't expect
About the ture. The triple helix unwinds and the chains
RCSB PDB Molecule of the Month proline to be this common, because it forms a
separate. Then, when this denatured mass of tan-
kink in the polypeptide chain that is difficult to
Using selected molecules from the PDB gled chains cools down, it soaks up all of the sur-
archive, each feature includes an introduction accommodate in typical globular proteins. But,
to the structure and function of the molecule,
rounding water like a sponge, forming gelatin.
as you can see on the next page, it seems to be
a discussion of its relevance to human health
and welfare, and suggestions for viewing and
just the right shape for this structural protein. Ropes and Ladders
accessing further details.
We make many different kinds of collagen,
The RCSB PDB Molecule of the Month is
read by students, teachers, and scientists
Vitamin C which form long ropes and tough sheets that are
worldwide at Hydroxyproline, which is critical for collagen used for structural support in mature animals
This April 2000 edition was written and stability, is created by modifying normal proline and as pathways for cellular movement during
illustrated by David S. Goodsell amino acids after the collagen chain is built. The development. All contain a long stretch of triple
(RCSB PDB and The Scripps reaction requires vitamin C to assist in the addi- helix connected to different types of ends. The
Research Institute).
tion of oxygen. Unfortunately, we cannot make simplest is merely a long triple helix, with blunt
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 ends. These "type I" collagen molecules associate A special amino acid sequence makes the tight colla-
the worldwide PDB side-by-side, like fibers in a rope, to form tough fib- gen triple helix particularly stable. Every third amino
(wwPDB; rils. These fibrils crisscross the space between nearly acid is a glycine, and many of the remaining amino
every one of our cells. acids are proline or hydroxyproline. A classic triple
The illustration above depicts a basement mem- helix is shown here, and may be viewed in the PDB
brane, which forms a tough surface that supports file 1cag. Notice how the glycine forms a tiny elbow
the skin and many organs. A different collagen– packed inside the helix, and notice how the proline
"type IV"–forms the structural basis of this mem- and hydroxyproline smoothly bend the chain back
brane. Type IV collagen has a globular head at one around the helix. In this structure, the researchers
end and an extra tail at the other. The heads bind placed a larger alanine amino acid in the position nor-
strongly together, head-to-head, and four collagen mally occupied by glycine, showing that it crowds the
molecules associate together through their tails, neighboring chains.
forming an X-shaped complex. Using these two
types of interactions, type IV collagen forms an 1bkv
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

This collagen helix contains a segment of human
References: collagen, and may be viewed in the PDB file 1bkv.
1cag: J. Bella, M. Eaton, B. Brodsky, H. M. Berman
(1994) Crystal and molecular structure of a collagen- Notice that the top half is very uniform, where the
like peptide at 1.9 A resolution. Science 266: 75-81
sequence is the ideal mixture of glycine and pro-
1bkv: R. Z. Kramer, J. Bella, P. Mayville, B. Brodsky, lines. At the bottom, the helix is less regular,
H. M. Berman (1999) Sequence dependent conforma-
tional variations of collagen triple-helical structure.
because many different amino acids are placed
Nat.Struct.Biol. 6: 454-457 between the equally-spaced glycines.