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Protein Science, Vol 6, Issue 3 534-542, Copyright © 1997 by Cold Spring Harbor Laboratory Press

ARTICLE

The counterreceptor binding site of human CD2 exhibits an extended surface patch with multiple conformations fluctuating with millisecond to microsecond motions

D. F. WYSS, K. T. DAYIE and G. WAGNER
Procept Inc., 840 Memorial Drive, Cambridge, Massachusetts 02139

We have used (15)N NMR relaxation experiments to probe, for the glycosylated human CD2 adhesion domain, the overall molecular motion, as well as very fast nanosecond-picosecond (ns-ps) and slow millisecond-microsecond (ms-{mu}s) internal motions. Using a novel analysis method that considers all residues, we obtained a correlation time for the overall motion of 9.5 +/- 0.3 ns. Surprisingly, we found a large contiguous patch of residues in the counterreceptor (CD58) binding site of human CD2 exhibiting slow conformational exchange motions (ms-{mu}s). On the other hand, almost none of the residues of the CD58 binding site display fast (ns-ps) internal motions of amplitudes larger than what is seen for well-ordered regions of the structure. Residues close to the N-glycosylation site, and the first N-acetylglucosamine of the high mannose glycan are as rigid as the protein core. Residues conserved in the immunoglobulin superfamily V-set domain are generally very rigid.
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This article has been cited by other articles:


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[Abstract] [Full Text] [PDF]


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