PMID- 10397151
OWN - NLM
STAT- MEDLINE
DCOM- 19991021
LR  - 20190826
IS  - 0165-2478 (Print)
IS  - 0165-2478 (Linking)
VI  - 68
IP  - 1
DP  - 1999 May 3
TI  - Biochemical analysis and crystallisation of Fc gamma RIIa, the low affinity
      receptor for IgG.
PG  - 17-23
AB  - Fc gamma RIIa is one of a family of specific cell surface receptors for
      immunoglobulin. Fc gamma RIIa, which binds immune complexes of certain IgG
      isotypes, plays important roles in immune homeostasis. However, the precise
      characteristics of IgG binding and three-dimensional structure of Fc gamma RIIa
      have not been reported. This study describes the affinity of the Fc gamma
      RIIa:IgG interaction as well as biochemical characterisation of recombinant Fc
      gamma RIIa that has been used to generate high quality crystals. Equilibrium
      binding analysis of the Fc gamma RII:IgG interaction found, IgG3 binds with an
      affinity of K(D) = 0.6 microM, as expected. Unlike other Fc gamma R, IgG4 also
      bound to Fc gamma RIIa, K(D) = 3 microM, clearly establishing Fc gamma RIIa as an
      IgG4 receptor. Biochemical analysis of mammalian and insect cell derived Fc gamma
      RIIa established the genuine N-terminus with Q being the first amino acid in the 
      sequence Q, A, A, A, P... extending the N-terminus further than previously
      thought. Furthermore, both potential N-linked glycosylation sites are occupied.
      Electrospray ionisation mass spectrometry (ESMS) indicate that the N-glycans of
      baculovirus derived Fc gamma RIIa are core mannose oligosaccharide side chains.
      Finally, we describe the first crystallisation of diffraction quality crystals of
      soluble Fc gamma RIIa. Orthorhombic crystals diffract X-rays beyond 2.1 A
      resolution in the space group P2(1)2(1)2 with cell dimensions a = 78.8 A, b =
      100.5 A, c = 27.8 A. This marks a significant advance towards understanding the
      three-dimensional structure of Fc gamma RIIa and related FcR proteins that share 
      high amino acid identity with Fc gamma RIIa.
FAU - Powell, M S
AU  - Powell MS
AD  - Helen M. Schutt Trust Laboratory for Immunology, Austin Research Institute,
      Austin and Repatriation Medical Centre, Heidelberg, Victoria, Australia.
FAU - Barton, P A
AU  - Barton PA
FAU - Emmanouilidis, D
AU  - Emmanouilidis D
FAU - Wines, B D
AU  - Wines BD
FAU - Neumann, G M
AU  - Neumann GM
FAU - Peitersz, G A
AU  - Peitersz GA
FAU - Maxwell, K F
AU  - Maxwell KF
FAU - Garrett, T P
AU  - Garrett TP
FAU - Hogarth, P M
AU  - Hogarth PM
LA  - eng
PT  - Journal Article
PL  - Netherlands
TA  - Immunol Lett
JT  - Immunology letters
JID - 7910006
RN  - 0 (Antigens, CD)
RN  - 0 (Fc gamma receptor IIA)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Receptors, IgG)
RN  - 0 (Recombinant Proteins)
SB  - IM
MH  - Animals
MH  - Antibody Affinity
MH  - Antigens, CD/*chemistry/*isolation & purification/metabolism
MH  - Binding Sites, Antibody
MH  - CHO Cells
MH  - Cricetinae
MH  - Crystallization
MH  - Crystallography, X-Ray
MH  - Humans
MH  - Immunoglobulin G/*metabolism
MH  - Mass Spectrometry
MH  - Receptors, IgG/*chemistry/*isolation & purification/metabolism
MH  - Recombinant Proteins/isolation & purification
MH  - Solubility
EDAT- 1999/07/09 00:00
MHDA- 1999/07/09 00:01
CRDT- 1999/07/09 00:00
PHST- 1999/07/09 00:00 [pubmed]
PHST- 1999/07/09 00:01 [medline]
PHST- 1999/07/09 00:00 [entrez]
AID - S0165-2478(99)00025-5 [pii]
AID - 10.1016/s0165-2478(99)00025-5 [doi]
PST - ppublish
SO  - Immunol Lett. 1999 May 3;68(1):17-23. doi: 10.1016/s0165-2478(99)00025-5.