1E4K

CRYSTAL STRUCTURE OF SOLUBLE HUMAN IGG1 FC FRAGMENT-FC-GAMMA RECEPTOR III COMPLEX

Summary for 1E4K

• Entry DOI: 10.2210/pdb1e4k/pdb
• Related: 1D5B 1D5I 1D6V 1E4J 1E4K 1FC1 2FCB
• Descriptor: FC FRAGMENT OF HUMAN IGG1, LOW AFFINITY IMMUNOGLOBULIN GAMMA FC RECEPTOR III, alpha-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: immune system, fc fragment, igg, receptor
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 3
• Total formula weight: 74104.02

Authors

Sondermann, P.,Huber, R.,Oosthuizen, V.,Jacob, U. (deposition date: 2000-07-07, release date: 2000-08-06, Last modification date: 2024-10-16)

Primary citation

Sondermann, P.,Huber, R.,Oosthuizen, V.,Jacob, U.
The 3.2A Crystal Structure of the Human Igg1 Fc Fragment-Fc-Gamma-Riii Complex
Nature, 406:267-, 2000

PubMed Abstract: The immune response depends on the binding of opsonized antigens to cellular Fc receptors and the subsequent initiation of various cellular effector functions of the immune system. Here we describe the crystal structures of a soluble Fc gamma receptor (sFc gammaRIII, CD16), an Fc fragment from human IgG1 (hFc1) and their complex. In the 1:1 complex the receptor binds to the two halves of the Fc fragment in contact with residues of the C gamma2 domains and the hinge region. Upon complex formation the angle between the two sFc gammaRIII domains increases significantly and the Fc fragment opens asymmetrically. The high degree of amino acid conservation between sFc gammaRIII and other Fc receptors, and similarly between hFc1 and related immunoglobulins, suggest similar structures and modes of association. Thus the described structure is a model for immune complex recognition and helps to explain the vastly differing affinities of other Fc gammaR-IgG complexes and the Fc epsilonRI alpha-IgE complex.

PubMed: 10917521
DOI: 10.1038/35018508

Experimental method

X-RAY DIFFRACTION (3.2 Å)