Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 1421 - 1434, Oktober 1976 Crystallographic Structural Studies of a Human Fc Fragment II. A Complete Model Based on a Fourier Map at 3.5 X Resolution* Johann DEISENHOFER, Peter M. COLMAN, Otto EPP and Robert HUBER Max-Planck-Institut fur Biochemie, Martinsried bei München und Physik Technischen Universität München (Received 15 July 1976) Summary: The crystal structure analysis of a human Fc fragment was pursued to 3.5 A resolution and a complete model was built and refined into the isomorphous Fourier map. The CH2 and Cn3 domains show the immunoglobulin fold, with C^3 being closely similar to CH!> but C H 2 intermediate in structure between V and CH3. The carbohydrate is rigidly attached to CH2, covering the C face. CH3 dimerizes as CH1-CL, but C H 2 has no contact to the second chain. Residues involved in the lateral CH3-CH3 and the longitudinal CH3-CH2 contact are conserved in Ig classes and sub-classes. In IgM and IgE the two C-terminal domains also show this characteristic distribution of contact residues. Kristallographische Studien an einem Fc-Fragment, 11. Ein vollständiges Modell nach einer Fourier-Synthese bei 3.5 Ä Auflösung Zusammenfassung: Die Kristallstrukturanalyse eines humanen Fc-Fragments wurde bis
hoppe-seyler's zeitschrift für physiologische chemie – de Gruyter
Published: Jan 1, 1976
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