The C alpha-H center dot center dot center dot O hydrogen bond: Adeterminant of stability and specificity in transmembrane helixinteractions

Senes A; Ubarretxena-Belandia I; Engelman DM

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The C alpha-H center dot center dot center dot O hydrogen bond: Adeterminant of stability and specificity in transmembrane helixinteractions

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The C alpha -(HO)-O-... hydrogen bond has been given Tittle attention as a determinant of transmembrane helix association. Stimulated by recent calculations suggesting that such bonds can be much stronger than has been supposed, we have analyzed 11 known membrane protein structures and found that apparent carbon hydrogen bonds cluster frequently at glycine-, serine-, and threonine-rich packing interfaces between transmembrane helices. Parallel right-handed helix-helix interactions appear to favor C alpha -(HO)-O-... bond formation. In particular, C alpha -(HO)-O-... interactions are frequent between helices having the structural motif of the glycophorin A dieter and the GxxxG pair. We suggest that C alpha -(HO)-O-... hydrogen bonds are important determinants of stability and, depending on packing, specificity in membrane protein folding.

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来源
《Proceedings of the National Academy of Sciences of the United States of America》 |2001年第16期|9056-9061|共6页
作者
Senes A; Ubarretxena-Belandia I; Engelman DM;
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作者单位

Engelman DM, Yale Univ, Dept Mol Biophys & Biochem, POB 208114, New Haven, CT 06520, USA;

Department of Otolaryngology, University Hospital VU, P.O. Box 7057, 1007 MB Amsterdam, The Netherlands;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
Membrane-proteins; Dimerization motif; Crystal-structure; Gxxxg motif; Association; Residues; Model; Asparagine; Resolution; Threonine;

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The C alpha-H center dot center dot center dot O hydrogen bond: Adeterminant of stability and specificity in transmembrane helixinteractions

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