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| The EMBO Journal
(2001) 20, 372–376, doi: 10.1093/emboj/20.3.372 |
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| A new twist in the collagen story—the type VI segmented supercoil |
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| Carlo Knupp and John M. Squire |
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Biological Structure and Function Section, Biomedical Sciences Division, Imperial College of Science, Technology & Medicine, London SW7 2AZ, UK To whom correspondence should be addressed John M. Squire, j.squire@ic.ac.uk Received 6 September 2000; Revised 5 December 2000; Accepted 5 December 2000. |
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| Abstract |
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Collagen occurs in two major forms: fibrillar and non-fibrillar. Non-fibrillar collagens are structurally more variable and relatively ill-understood. In this work we analysed the amino acid sequence of type VI collagen, a non-fibrillar collagen that forms antiparallel dimers. A sequence motif was discovered that gives rise to systematic molecular coiling. There is a common periodicity ( 23 or 2  23 residues) in the charged amino acids, in the prolines and in the discontinuities in the Gly-X-Y triplets. In addition, there is a different periodicity (21 amino acids) in the apolar groups. The two repeats mean that the only way to simultaneously maximize both the hydrophobic and polar interactions during dimer formation is with the molecules antiparallel, overlapped by 75 nm as observed, and supercoiled. The alternating proline-rich and charge-rich patches, often together with discontinuities in the Gly-X-Y sequences, coincide with each half-turn of the supercoil, thus breaking it into segments. We have termed this structure the collagen segmented supercoil. The segmented supercoil and variants may be common aggregation motifs for the non-fibrillar collagens. |
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| Keywords: amino acid sequence analysis, collagen IV, collagen VI, collagen segmented supercoil, non-fibrillar collagen |
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