1. The seven-stranded beta-barrel structure of apo-neocarzinostatin as compared to the immunoglobulin domain
- Author
-
Elisabeth Adjadj, V. Favoudon, Jean-Marc Lhoste, Eric Quiniou, and Joël Mispelter
- Subjects
Binding Sites ,Magnetic Resonance Spectroscopy ,biology ,Stereochemistry ,Chemistry ,Molecular Sequence Data ,Active site ,Immunoglobulins ,General Medicine ,Nuclear magnetic resonance spectroscopy ,Immunoglobulin domain ,Antiparallel (biochemistry) ,Biochemistry ,Protein Structure, Tertiary ,Crystallography ,Protein structure ,Models, Chemical ,X-Ray Diffraction ,Zinostatin ,biology.protein ,Amino Acid Sequence ,Binding site ,Protons ,Peptide sequence ,Protein secondary structure - Abstract
The three-dimensional structure of apo-NCS, as revealed by proton NMR, is based on an antiparallel seven-stranded beta-barrel. This fold is frequently encountered in protein structures, especially for immunoglobulin domains. The strands forming the barrel are joined by flexible loops of which three are implicated in the ligand binding site of these proteins. In this paper a preliminary comparison is given with respect to the static and dynamic properties of both the constant beta-barrel and the active loops for apo-NCS and the variable VH domain of an immunoglobulin Fab' fragment.
- Published
- 1992