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The counterreceptor binding site of human CD2 exhibits an extended surface patch with multiple conformations fluctuating with millisecond to microsecond motions
Author(s) -
Wyss Daniel F.,
Dayie Kwaku T.,
Wagner Gerhard
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560060303
Subject(s) - microsecond , millisecond , chemical physics , molecular physics , physics , chemistry , biophysics , materials science , optics , biology , quantum mechanics
We have used 15N 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‐/xs) 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‐ytis). 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.