Climate, traffic-related air pollutants, and asthma prevalence in middle-school children in Taiwan

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Title:	Climate, traffic-related air pollutants, and asthma prevalence in middle-school children in Taiwan
Authors:	Guo, YLL;Lin, YC;Sung, FC;Huang, SL;Ko, YC;Lai, JS;Su, HJ;Shaw, CK;Lin, RS;Dockery, DW
Contributors:	公共衛生學院職安系;Natl Taiwan Univ, Inst Epidemiol, Taipei 10764, Taiwan;Natl Cheng Kung Univ, Tainan 70101, Taiwan;Natl Taiwan Univ, Inst Environm Hlth, Taipei 10764, Taiwan;Natl Yang Ming Univ, Inst Environm Hlth Sci, Taipei 112, Taiwan;Kaohsiung Med Coll, Dept Publ Hlth, Kaohsiung, Taiwan;China Med Coll, Sch Occupat Safety & Hlth, Taichung, Taiwan;Tzu Chi Coll Med & Humanities, Dept Publ Hlth, Hua Lien, Taiwan;Harvard Univ, Sch Publ Hlth, Dept Environm Hlth Sci, Boston, MA USA
Date:	1999
Issue Date:	2010-09-24 14:00:19 (UTC+8)
Publisher:	US DEPT HEALTH HUMAN SCIENCES PUBLIC HEALTH SCIENCE
Abstract:	The solution structure and dynamics of G1TE, a nonphosphorylated cyclic peptide inhibitor for the Grb2 SH2 domain, was determined using two-dimensional NMR and simulated annealing methods. G1TE consists of 10 amino acids and a C-terminal Cys cyclized through its side-chain sulfur atom by a thioether linkage to its N terminus. The results indicate that G1TE assumes a circle-like shape in solution in which all the side chains are protruding outside, and none of the residues are involved in intramolecular hydrogen bonding. The average root-mean-square deviations were found to be 0.41 +/- 0.11 Angstrom for the backbone heavy atoms C, C alpha, and N, and 1.03 +/- 0.14 Angstrom for all heavy atoms in a family of 10 structures. N-15 relaxation measurements indicate that G1TE has rather restricted dynamics in the fast time scale within its backbone. However, residues Tyr3, Val6, and Gly7 may be involved in a possible conformational exchange. The structural comparison between G1TE in solution and the BCR-Abl phosphopeptide bound to Grb2 SH2 domain revealed that G1TE may form a larger circle-like binding surface than the BCR-Abl phosphopeptide in the bound form. Also, the restricted backbone dynamics of G1TE may result in a reduced loss of entropy and can compensate for the absence of a phosphate group at the Tyr3 position. These structural and dynamic properties of G1TE may provide a molecular basis for understanding its interactions with the Grb2 SH2 domain. (C) 1999 Academic Press.
Relation:	ENVIRONMENTAL HEALTH PERSPECTIVES 107(12):1001-1006
Appears in Collections:	[Department and Graduate of Health Services Administration] Journal articles

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