共 25 条
A transmembrane form of annexin XII detected by site-directed spin labeling
被引:89
作者:
Langen, R
Isas, JM
Hubbell, WL
Haigler, HT
[1
]
机构:
[1] Univ Calif Irvine, Dept Physiol & Biophys, Irvine, CA 92697 USA
[2] Univ Calif Los Angeles, Jules Stein Eye Inst, Los Angeles, CA 90095 USA
[3] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA
来源:
关键词:
D O I:
10.1073/pnas.95.24.14060
中图分类号:
O [数理科学和化学];
P [天文学、地球科学];
Q [生物科学];
N [自然科学总论];
学科分类号:
07 ;
0710 ;
09 ;
摘要:
Previous studies of the annexin family of Ca2+ binding proteins identified a soluble monomer in the absence of Ca2+ and a trimer adsorbed on the membrane surface in the presence of Ca2+. On the basis of site-directed spin-labeling studies of annexin XII at low pH, we now report a membrane-inserted form of the protein with a dramatically different structure. The data suggest that upon insertion a continuous transmembrane alpha-helix is reversibly formed from a helix-loop-helix motif in the solution structure. Other regions with similar membrane-insertion potential were identified in the amino acid sequence, and we propose that the corresponding helices come together to form an aqueous pore that mediates the ion channel activity reported for several annexins.
引用
收藏
页码:14060 / 14065
页数:6
相关论文