1USD

human VASP tetramerisation domain L352M

Summary for 1USD

• Entry DOI: 10.2210/pdb1usd/pdb
• Related: 1EGX 1JNG 1USE
• Descriptor: VASODILATOR-STIMULATED PHOSPHOPROTEIN (2 entities in total)
• Functional Keywords: signaling protein, phosphorylation, actin-binding, kinase
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: P50552
• Total number of polymer chains: 1
• Total formula weight: 5315.04

Authors

Kuhnel, K.,Jarchau, T.,Wolf, E.,Schlichting, I.,Walter, U.,Wittinghofer, A.,Strelkov, S.V. (deposition date: 2003-11-21, release date: 2004-11-11, Last modification date: 2024-05-08)

Primary citation

Kuhnel, K.,Jarchau, T.,Wolf, E.,Schlichting, I.,Walter, U.,Wittinghofer, A.,Strelkov, S.V.
The Vasp Tetramerization Domain is a Right-Handed Coiled Coil Based on a 15-Residue Repeat
Proc.Natl.Acad.Sci.USA, 101:17027-, 2004

PubMed Abstract: The vasodilator-stimulated phosphoprotein (VASP) is a key regulator of actin dynamics. We have determined the 1.3-A resolution crystal structure of the 45-residue-long tetramerization domain (TD) from human VASP. This domain forms a right-handed alpha-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 degrees C.

PubMed: 15569942
DOI: 10.1073/PNAS.0403069101

Experimental method

X-RAY DIFFRACTION (1.7 Å)