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1D7M

COILED-COIL DIMERIZATION DOMAIN FROM CORTEXILLIN I

Summary for 1D7M
Entry DOI10.2210/pdb1d7m/pdb
Related2ZTA
DescriptorCORTEXILLIN I (2 entities in total)
Functional Keywordscoiled-coil, coiled-coil trigger site, alpha helix, dimerization, contractile protein
Biological sourceDictyostelium discoideum
Total number of polymer chains2
Total formula weight23246.56
Authors
Burkhard, P.,Kammerer, R.A.,Steinmetz, M.O.,Bourenkov, G.P.,Aebi, U. (deposition date: 1999-10-19, release date: 2000-03-27, Last modification date: 2024-02-07)
Primary citationBurkhard, P.,Kammerer, R.A.,Steinmetz, M.O.,Bourenkov, G.P.,Aebi, U.
The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges.
Structure Fold.Des., 8:223-230, 2000
Cited by
PubMed Abstract: The parallel two-stranded alpha-helical coiled coil is the most frequently encountered subunit-oligomerization motif in proteins. The simplicity and regularity of this motif have made it an attractive system to explore some of the fundamental principles of protein folding and stability and to test the principles of de novo design.
PubMed: 10745004
DOI: 10.1016/S0969-2126(00)00100-3
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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