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| SEQUENCE SPECIFICITY IN THE DIMERIZATION OF TRANSMEMBRANE ALPHA-HELICES |
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| Author(s): LEMMON MA, FLANAGAN JM, TREUTLEIN HR, ZHANG J, ENGELMAN DM |
| Source: BIOCHEMISTRY Volume: 31 Issue: 51 Pages: 12719-12725 Published: DEC 29 1992 |
| Times Cited: 332 References: 39 |
| Abstract: While several reports have suggested a role for helix-helix interactions in membrane protein oligomerization, there are few direct biochemical data bearing on this subject. Here, using mutational analysis, we show that dimerization of the transmembrane alpha-helix of glycophorin A in a detergent environment is spontaneous and highly specific. Very subtle changes in the side-chain structure at certain sensitive positions disrupt the helix-helix association. These sensitive positions occur at approximately every 3.9 residues along the helix, consistent with their comprising the interface of a closely fit transmembranous supercoil of alpha-helices. By contrast with other reported cases of interactions between transmembrane helices, the set of interfacial residues in this case contains no highly polar groups. Amino acids with aliphatic side chains define much of the interface, indicating that precise packing interactions between the helices may provide much of the energy for association. These data highlight the potential general importance of specific interactions between the hydrophobic anchors of integral membrane proteins. |
| Document Type: Note |
| Language: English |
Addresses:
1. YALE UNIV, PEABODY MUSEUM NAT HIST, DEPT MOLEC BIOPHYS & BIOCHEM, 260 WHITNEY AVE, POB 6666, NEW HAVEN, CT 06511 USA |
| Publisher: AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: KE606 |
| ISSN: 0006-2960 |
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