NMR structure of a parallel homotrimeric coiled coil

S. A. Dames; R. A. Kammerer; R. Wiltscheck; J. Engel; A. T. Alexandrescu

doi:10.1038/1382

NMR structure of a parallel homotrimeric coiled coil

S. A. Dames
, R. A. Kammerer
, R. Wiltscheck
, J. Engel
, A. T. Alexandrescu

Research output: Contribution to journal › Article › peer-review

Abstract

The solution structure of the oligomerization domain of cartilage matrix protein (also known as matrilin-1) has been determined by heteronuclear NMR spectroscopy. The domain folds into a parallel, disulfide-linked, three- stranded, α-helical coiled coil, spanning five heptad repeats in the amino acid sequence. The sequence of the first two heptad repeats shows some deviations from the consensus of hydrophobic and hydrophilic residue preferences. While the corresponding region of the coiled coil has a higher intrinsic flexibility, backbone α-helix and superhelix parameters are consistent with a regular coiled coil structure.

Original language	English
Pages (from-to)	687-691
Number of pages	4
Journal	Nature Structural Biology
Volume	5
Issue number	8
DOIs	https://doi.org/10.1038/1382
Publication status	Published - 1998

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title = "NMR structure of a parallel homotrimeric coiled coil",

abstract = "The solution structure of the oligomerization domain of cartilage matrix protein (also known as matrilin-1) has been determined by heteronuclear NMR spectroscopy. The domain folds into a parallel, disulfide-linked, three- stranded, α-helical coiled coil, spanning five heptad repeats in the amino acid sequence. The sequence of the first two heptad repeats shows some deviations from the consensus of hydrophobic and hydrophilic residue preferences. While the corresponding region of the coiled coil has a higher intrinsic flexibility, backbone α-helix and superhelix parameters are consistent with a regular coiled coil structure.",

author = "Dames, \{S. A.\} and Kammerer, \{R. A.\} and R. Wiltscheck and J. Engel and Alexandrescu, \{A. T.\}",

year = "1998",

doi = "10.1038/1382",

language = "English",

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pages = "687--691",

journal = "Nature Structural Biology",

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T1 - NMR structure of a parallel homotrimeric coiled coil

AU - Dames, S. A.

AU - Kammerer, R. A.

AU - Wiltscheck, R.

AU - Engel, J.

AU - Alexandrescu, A. T.

PY - 1998

Y1 - 1998

N2 - The solution structure of the oligomerization domain of cartilage matrix protein (also known as matrilin-1) has been determined by heteronuclear NMR spectroscopy. The domain folds into a parallel, disulfide-linked, three- stranded, α-helical coiled coil, spanning five heptad repeats in the amino acid sequence. The sequence of the first two heptad repeats shows some deviations from the consensus of hydrophobic and hydrophilic residue preferences. While the corresponding region of the coiled coil has a higher intrinsic flexibility, backbone α-helix and superhelix parameters are consistent with a regular coiled coil structure.

AB - The solution structure of the oligomerization domain of cartilage matrix protein (also known as matrilin-1) has been determined by heteronuclear NMR spectroscopy. The domain folds into a parallel, disulfide-linked, three- stranded, α-helical coiled coil, spanning five heptad repeats in the amino acid sequence. The sequence of the first two heptad repeats shows some deviations from the consensus of hydrophobic and hydrophilic residue preferences. While the corresponding region of the coiled coil has a higher intrinsic flexibility, backbone α-helix and superhelix parameters are consistent with a regular coiled coil structure.

U2 - 10.1038/1382

DO - 10.1038/1382

M3 - Article

C2 - 9699631

VL - 5

SP - 687

EP - 691

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 8

ER -

NMR structure of a parallel homotrimeric coiled coil

Abstract

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