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Structures of the αL I Domain and Its Complex with ICAM-1 Reveal a Shape-Shifting Pathway for Integrin Regulation
| Content Provider | PubMed Central |
|---|---|
| Author | Shimaoka, Motomu Xiao, Tsan Liu, Jin-huan Yang, Yuting Dong, Yicheng Jun, Chang-duk Mccormack, Alison Zhang, Rongguang Joachimiak, Andrzej Takagi, Junichi Wang, Jia-huai Springer, Timothy A. |
| Copyright Year | 2003 |
| Abstract | The structure of the I domain of integrin αLβ 2 bound to the Ig superfamily ligand ICAM-1 reveals the open ligand binding conformation and the first example of an integrin-IgSF interface. The I domain Mg2+ directly coordinates Glu-34 of ICAM-1, and a dramatic swing of I domain residue Glu-241 enables a critical salt bridge. Liganded and unliganded structures for both high- and intermediate-affinity mutant I domains reveal that ligand binding can induce conformational change in the αL I domain and that allosteric signals can convert the closed conformation to intermediate or open conformations without ligand binding. Pulling down on the C-terminal α7 helix with introduced disulfide bonds ratchets the β6-α7 loop into three different positions in the closed, intermediate, and open conformations, with a progressive increase in affinity. |
| Starting Page | 99 |
| File Format | |
| ISSN | 10974172 |
| e-ISSN | 10974172 |
| Journal | Cell |
| Issue Number | 1 |
| Volume Number | 112 |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry, Genetics and Molecular Biology |
