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- Publisher Website: 10.1016/j.molcel.2008.06.022
- Scopus: eid_2-s2.0-48349146151
- PMID: 18691975
- WOS: WOS:000258556500016
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Article: An Unusual Allosteric Mobility of the C-Terminal Helix of a High-Affinity αL Integrin I Domain Variant Bound to ICAM-5
Title | An Unusual Allosteric Mobility of the C-Terminal Helix of a High-Affinity αL Integrin I Domain Variant Bound to ICAM-5 |
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Authors | |
Keywords | PROTEIN SIGNALING |
Issue Date | 2008 |
Publisher | Cell Press. The Journal's web site is located at http://www.elsevier.com/locate/molcel |
Citation | Molecular Cell, 2008, v. 31 n. 3, p. 432-437 How to Cite? |
Abstract | Integrins are cell surface receptors that transduce signals bidirectionally across the plasma membrane. The key event of integrin signaling is the allosteric regulation between its ligand-binding site and the C-terminal helix (α7) of integrin's inserted (I) domain. A significant axial movement of the α7 helix is associated with the open, active conformation of integrins. We describe the crystal structure of an engineered high-affinity I domain from the integrin αLβ2 (LFA-1) α subunit in complex with the N-terminal two domains of ICAM-5, an adhesion molecule expressed in telencephalic neurons. The finding that the α7 helix swings out and inserts into a neighboring I domain in an upside-down orientation in the crystals implies an intrinsically unusual mobility of this helix. This remarkable feature allows the α7 helix to trigger integrin's large-scale conformational changes with little energy penalty. It serves as a mechanistic example of how a weakly bound adhesion molecule works in signaling. © 2008 Elsevier Inc. All rights reserved. |
Persistent Identifier | http://hdl.handle.net/10722/171770 |
ISSN | 2023 Impact Factor: 14.5 2023 SCImago Journal Rankings: 9.332 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Zhang, H | en_US |
dc.contributor.author | Casasnovas, JM | en_US |
dc.contributor.author | Jin, M | en_US |
dc.contributor.author | Liu, Jh | en_US |
dc.contributor.author | Gahmberg, CG | en_US |
dc.contributor.author | Springer, TA | en_US |
dc.contributor.author | Wang, Jh | en_US |
dc.date.accessioned | 2012-10-30T06:16:56Z | - |
dc.date.available | 2012-10-30T06:16:56Z | - |
dc.date.issued | 2008 | en_US |
dc.identifier.citation | Molecular Cell, 2008, v. 31 n. 3, p. 432-437 | en_US |
dc.identifier.issn | 1097-2765 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171770 | - |
dc.description.abstract | Integrins are cell surface receptors that transduce signals bidirectionally across the plasma membrane. The key event of integrin signaling is the allosteric regulation between its ligand-binding site and the C-terminal helix (α7) of integrin's inserted (I) domain. A significant axial movement of the α7 helix is associated with the open, active conformation of integrins. We describe the crystal structure of an engineered high-affinity I domain from the integrin αLβ2 (LFA-1) α subunit in complex with the N-terminal two domains of ICAM-5, an adhesion molecule expressed in telencephalic neurons. The finding that the α7 helix swings out and inserts into a neighboring I domain in an upside-down orientation in the crystals implies an intrinsically unusual mobility of this helix. This remarkable feature allows the α7 helix to trigger integrin's large-scale conformational changes with little energy penalty. It serves as a mechanistic example of how a weakly bound adhesion molecule works in signaling. © 2008 Elsevier Inc. All rights reserved. | en_US |
dc.language | eng | en_US |
dc.publisher | Cell Press. The Journal's web site is located at http://www.elsevier.com/locate/molcel | en_US |
dc.relation.ispartof | Molecular Cell | en_US |
dc.subject | PROTEIN | - |
dc.subject | SIGNALING | - |
dc.subject.mesh | Allosteric Regulation | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Antigens, Cd11a - Chemistry - Metabolism | en_US |
dc.subject.mesh | Cho Cells | en_US |
dc.subject.mesh | Cell Adhesion Molecules - Chemistry - Metabolism | en_US |
dc.subject.mesh | Cricetinae | en_US |
dc.subject.mesh | Cricetulus | en_US |
dc.subject.mesh | Crystallography, X-Ray | en_US |
dc.subject.mesh | Models, Molecular | en_US |
dc.subject.mesh | Mutant Proteins - Chemistry - Metabolism | en_US |
dc.subject.mesh | Protein Binding | en_US |
dc.subject.mesh | Protein Structure, Secondary | en_US |
dc.subject.mesh | Protein Structure, Tertiary | en_US |
dc.title | An Unusual Allosteric Mobility of the C-Terminal Helix of a High-Affinity αL Integrin I Domain Variant Bound to ICAM-5 | en_US |
dc.type | Article | en_US |
dc.identifier.email | Zhang, H:hzhang20@hku.hk | en_US |
dc.identifier.authority | Zhang, H=rp00306 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1016/j.molcel.2008.06.022 | en_US |
dc.identifier.pmid | 18691975 | - |
dc.identifier.scopus | eid_2-s2.0-48349146151 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-48349146151&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 31 | en_US |
dc.identifier.issue | 3 | en_US |
dc.identifier.spage | 432 | en_US |
dc.identifier.epage | 437 | en_US |
dc.identifier.isi | WOS:000258556500016 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Zhang, H=7409196101 | en_US |
dc.identifier.scopusauthorid | Casasnovas, JM=7004669758 | en_US |
dc.identifier.scopusauthorid | Jin, M=7202559652 | en_US |
dc.identifier.scopusauthorid | Liu, Jh=36066228400 | en_US |
dc.identifier.scopusauthorid | Gahmberg, CG=7005887684 | en_US |
dc.identifier.scopusauthorid | Springer, TA=35450639400 | en_US |
dc.identifier.scopusauthorid | Wang, Jh=7701330874 | en_US |
dc.identifier.citeulike | 3114839 | - |
dc.identifier.issnl | 1097-2765 | - |