1FNL

CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF A HUMAN FCGRIII

Summary for 1FNL

• Entry DOI: 10.2210/pdb1fnl/pdb
• Descriptor: LOW AFFINITY IMMUNOGLOBULIN GAMMA FC REGION RECEPTOR III-B, MERCURY (II) ION (3 entities in total)
• Functional Keywords: beta sandwich, immunoglobulin-like, receptor, immune system receptor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 20405.47

Authors

Zhang, Y.,Boesen, C.C.,Radaev, S.,Brooks, A.G.,Fridman, W.H.,Sautes-Fridman, C.,Sun, P.D. (deposition date: 2000-08-22, release date: 2000-11-22, Last modification date: 2024-10-30)

Primary citation

Zhang, Y.,Boesen, C.C.,Radaev, S.,Brooks, A.G.,Fridman, W.H.,Sautes-Fridman, C.,Sun, P.D.
Crystal structure of the extracellular domain of a human Fc gamma RIII.
Immunity, 13:387-395, 2000

PubMed Abstract: Fc receptors play a major role in immune defenses against pathogens and in inflammatory processes. The crystal structure of a human immunoglobulin receptor, FcgammaRIIIb, has been determined to 1.8 A resolution. The overall fold consists of two immunoglobulin-like domains with an acute interdomain hinge angle of approximately 50 degrees. Trp-113, wedged between the N-terminal D1 and the C-terminal D2 domains, appears to further restrict the hinge angle. The putative Fc binding region of the receptor carries a net positive charge complementary to the negative-charged receptor binding regions on Fc. A 1:1 binding stoichiometry between the receptor and Fc was measured by both the equilibrium and nonequilibrium size-exclusion chromatography. Two separate parallel dimers are observed in the crystal lattice, offering intriguing models for receptor aggregation.

PubMed: 11021536
DOI: 10.1016/S1074-7613(00)00038-8

Experimental method

X-RAY DIFFRACTION (1.8 Å)