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  The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat

Kühnel, K., Jarchau, T., Wolf, E., Schlichting, I., Walter, U., Wittinghofer, A., et al. (2004). The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat. Proceedings of the National Academy of Sciences of the United States of America, 101(49), 17027-17032. doi:10.1073/pnas.0403069101.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002A-30F1-F Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002A-3142-4
Genre: Journal Article
Alternative Title : The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat

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 Creators:
Kühnel, Karin1, Author           
Jarchau, Thomas, Author
Wolf, Eva, Author
Schlichting, Ilme1, 2, Author           
Walter, Ulrich, Author
Wittinghofer, Alfred2, Author           
Strelkov, Sergei V., Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: The vasodilator-stimulated phosphoprotein (VASP) is a key regulator of actin dynamics. We have determined the 1.3-Å resolution crystal structure of the 45-residue-long tetramerization domain (TD) from human VASP. This domain forms a right-handed -helical coiled-coil structure with a similar degree of supercoiling as found in the widespread left-handed coiled coils with heptad repeats. The basis for the right-handed geometry of VASP TD is a 15-residue repeat in its amino acid sequence, which reveals a characteristic pattern of hydrophobic residues. Hydrophobic interactions and a network of salt bridges render VASP TD highly thermostable with a melting point of 120°C.

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Language(s): eng - English
 Dates: 2004-05-112004-10-152004-11-292004-12-07
 Publication Status: Issued
 Pages: 5
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 665667
DOI: 10.1073/pnas.0403069101
URI: http://www.ncbi.nlm.nih.gov/pubmed/15569942
URI: http://www.pnas.org/content/101/49/17027
URI: http://www.pnas.org/content/101/49/17027.full
Other: 6280
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: National Academy of Sciences
Pages: - Volume / Issue: 101 (49) Sequence Number: - Start / End Page: 17027 - 17032 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230