1MOT

NMR Structure Of Extended Second Transmembrane Domain Of Glycine Receptor alpha1 Subunit in SDS Micelles

Summary for 1MOT

• Entry DOI: 10.2210/pdb1mot/pdb
• NMR Information: BMRB: 5607
• Descriptor: Glycine Receptor alpha-1 CHAIN (1 entity in total)
• Functional Keywords: glycine receptor, second transmembrane domain, micelles, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein: P23415
• Total number of polymer chains: 1
• Total formula weight: 2804.25

Authors

Yushmanov, V.E.,Mandal, P.K.,Liu, Z.,Tang, P.,Xu, Y. (deposition date: 2002-09-09, release date: 2003-09-23, Last modification date: 2024-05-22)

Primary citation

Yushmanov, V.E.,Mandal, P.K.,Liu, Z.,Tang, P.,Xu, Y.
NMR Structure and Backbone Dynamics of the Extended Second Transmembrane Domain of the Human Neuronal Glycine Receptor Alpha1 Subunit
Biochemistry, 42:3989-3995, 2003

PubMed Abstract: The structure and backbone dynamics of an extended second transmembrane segment (TM2e) of the human neuronal glycine receptor alpha(1) subunit in sodium dodecyl sulfate micelles were studied by (1)H and (15)N solution-state NMR. The 28-amino acid segment contained the consensus TM2 domain plus part of the linker between the second and third transmembrane domains. The presence of a well-structured helical region of at least 13 amino acids long and an unstructured region near the linker was evident from the proton chemical shifts and the pattern of midrange nuclear Overhauser effects (NOE). (15)N relaxation rate constants, R(1) and R(2), and (15)N-[(1)H] NOE indicated restricted internal motions in the helical region with NOE values between 0.6 and 0.8. The squared order parameter (S(2)), the effective correlation time for fast internal motions (tau(e)), and the global rotational correlation time (tau(m)) were calculated for all TM2e backbone N-H bonds using the model-free approach. The S(2) values ranged about 0.75-0.86, and the tau(e) values were below 100 ps for most of the residues in the helical region. The tau(m) value, calculated from the dynamics of the helical region, was 5.1 ns. The S(2) values decreased to 0.1, and the tau(e) values sharply increased up to 1.2 ns at the linker near the C-terminus, indicating that the motion of this region is unrestricted. The results suggest a relatively high degree of motional freedom of TM2e in micelles and different propensities of the N- and C-terminal moieties of the transmembrane domain to assume stable helical structures.

PubMed: 12667090
DOI: 10.1021/bi026767g

Experimental method

SOLUTION NMR