2AKF

Crystal structure of the coiled-coil domain of coronin 1

Summary for 2AKF

• Entry DOI: 10.2210/pdb2akf/pdb
• Descriptor: Coronin-1A, ZINC ION (3 entities in total)
• Functional Keywords: coiled coil, coronin 1, protein binding
• Cellular location: Cytoplasm, cytoskeleton: O89053
• Total number of polymer chains: 3
• Total formula weight: 11659.52

Authors

Kammerer, R.A.,Kostrewa, D.,Progias, P.,Honnappa, S.,Avila, D.,Lustig, A.,Winkler, F.K.,Pieters, J.,Steinmetz, M.O. (deposition date: 2005-08-03, release date: 2005-09-27, Last modification date: 2024-03-13)

Primary citation

Kammerer, R.A.,Kostrewa, D.,Progias, P.,Honnappa, S.,Avila, D.,Lustig, A.,Winkler, F.K.,Pieters, J.,Steinmetz, M.O.
A conserved trimerization motif controls the topology of short coiled coils
Proc.Natl.Acad.Sci.Usa, 102:13891-13896, 2005

PubMed Abstract: In recent years, short coiled coils have been used for applications ranging from biomaterial to medical sciences. For many of these applications knowledge of the factors that control the topology of the engineered protein systems is essential. Here, we demonstrate that trimerization of short coiled coils is determined by a distinct structural motif that encompasses specific networks of surface salt bridges and optimal hydrophobic packing interactions. The motif is conserved among intracellular, extracellular, viral, and synthetic proteins and defines a universal molecular determinant for trimer formation of short coiled coils. In addition to being of particular interest for the biotechnological production of candidate therapeutic proteins, these findings may be of interest for viral drug development strategies.

PubMed: 16172398
DOI: 10.1073/pnas.0502390102

Experimental method

X-RAY DIFFRACTION (1.2 Å)