STRUCTURAL DETAILS OF NKR-P1D/CLRB INTERACTION ELUCIDATED BY CHEMICAL CROSS-LINKING AND MASS SPECTROMETRY.

摘要

Using recently resolved structures of extracellular domains of NKR-P1A and Clrg receptors bearing 86percent and 76percent sequence identity with NKR-P1D and Clrb respectively, we were able to build homology models of both NKR-P1D and Clrb and a model of the interacting pair (Fig. 3A). Part of the data obtained from cross-linking experiments fitted nicely into the model of homodimers of both proteins interacting in a face-to-face fashion as would be expected; however significant portion of the observed cross-links could not be explained by this model. In order to allow for these data we suggest that these receptors do not only interact in the face-to-face fashion but also in a chain-like or cluster-like fashion with each homodimer contacting two homodimers of the second protein at the same time (Fig. 3B). To our knowledge this would be the first interaction of this kind observed for this type of receptors.