1mot

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{{STRUCTURE_1mot| PDB=1mot | SCENE= }}
{{STRUCTURE_1mot| PDB=1mot | SCENE= }}
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'''NMR Structure Of Extended Second Transmembrane Domain Of Glycine Receptor alpha1 Subunit in SDS Micelles'''
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===NMR Structure Of Extended Second Transmembrane Domain Of Glycine Receptor alpha1 Subunit in SDS Micelles===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12667090 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12667090}}
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1MOT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOT OCA].
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1MOT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOT OCA].
==Reference==
==Reference==
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[[Category: Nmr]]
[[Category: Nmr]]
[[Category: Second transmembrane domain]]
[[Category: Second transmembrane domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:31:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:36:42 2008''

Revision as of 21:36, 2 July 2008

Image:1mot.png

Template:STRUCTURE 1mot

Contents

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

Template:ABSTRACT PUBMED 12667090

Disease

Known disease associated with this structure: Hyperekplexia and spastic paraparesis OMIM:[138491], Startle disease, autosomal recessive OMIM:[138491], Startle disease/hyperekplexia, autosomal dominant OMIM:[138491]

About this Structure

1MOT is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

NMR structure and backbone dynamics of the extended second transmembrane domain of the human neuronal glycine receptor alpha1 subunit., Yushmanov VE, Mandal PK, Liu Z, Tang P, Xu Y, Biochemistry. 2003 Apr 8;42(13):3989-95. PMID:12667090

Page seeded by OCA on Thu Jul 3 00:36:42 2008

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