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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

TitleAn Unusual Allosteric Mobility of the C-Terminal Helix of a High-Affinity αL Integrin I Domain Variant Bound to ICAM-5
Authors
Issue Date2008
PublisherCell 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?
AbstractIntegrins 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 Identifierhttp://hdl.handle.net/10722/171770
ISSN
2015 Impact Factor: 13.958
2015 SCImago Journal Rankings: 13.658
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhang, Hen_US
dc.contributor.authorCasasnovas, JMen_US
dc.contributor.authorJin, Men_US
dc.contributor.authorLiu, Jhen_US
dc.contributor.authorGahmberg, CGen_US
dc.contributor.authorSpringer, TAen_US
dc.contributor.authorWang, Jhen_US
dc.date.accessioned2012-10-30T06:16:56Z-
dc.date.available2012-10-30T06:16:56Z-
dc.date.issued2008en_US
dc.identifier.citationMolecular Cell, 2008, v. 31 n. 3, p. 432-437en_US
dc.identifier.issn1097-2765en_US
dc.identifier.urihttp://hdl.handle.net/10722/171770-
dc.description.abstractIntegrins 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.languageengen_US
dc.publisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/molcelen_US
dc.relation.ispartofMolecular Cellen_US
dc.subject.meshAllosteric Regulationen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntigens, Cd11a - Chemistry - Metabolismen_US
dc.subject.meshCho Cellsen_US
dc.subject.meshCell Adhesion Molecules - Chemistry - Metabolismen_US
dc.subject.meshCricetinaeen_US
dc.subject.meshCricetulusen_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMutant Proteins - Chemistry - Metabolismen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.titleAn Unusual Allosteric Mobility of the C-Terminal Helix of a High-Affinity αL Integrin I Domain Variant Bound to ICAM-5en_US
dc.typeArticleen_US
dc.identifier.emailZhang, H:hzhang20@hku.hken_US
dc.identifier.authorityZhang, H=rp00306en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.molcel.2008.06.022en_US
dc.identifier.pmid18691975-
dc.identifier.scopuseid_2-s2.0-48349146151en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-48349146151&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume31en_US
dc.identifier.issue3en_US
dc.identifier.spage432en_US
dc.identifier.epage437en_US
dc.identifier.isiWOS:000258556500016-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridZhang, H=7409196101en_US
dc.identifier.scopusauthoridCasasnovas, JM=7004669758en_US
dc.identifier.scopusauthoridJin, M=7202559652en_US
dc.identifier.scopusauthoridLiu, Jh=36066228400en_US
dc.identifier.scopusauthoridGahmberg, CG=7005887684en_US
dc.identifier.scopusauthoridSpringer, TA=35450639400en_US
dc.identifier.scopusauthoridWang, Jh=7701330874en_US
dc.identifier.citeulike3114839-

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