Related ArticlesNMR analysis of structure and dynamics of the cytosolic tails of integrin alpha IIb beta 3 in aqueous solution.
Biochemistry. 2001 Jun 26;40(25):7498-508
Authors: Ulmer TS, Yaspan B, Ginsberg MH, Campbell ID
The structural and dynamic properties of the cytosolic tails of the adhesion receptor integrin alphaIIbbeta3, fused to a coiled-coil construct via (Gly)(3) linkers, were studied in aqueous solution by nuclear magnetic resonance (NMR) spectroscopy. Both tails were largely flexible and unstructured, although, in the beta3 tail, residues Arg(724)-Ala(735) have a propensity to form a helical structure and residues Asn(744)-Tyr(747) (NPLY) have a propensity to adopt reverse-turn conformations. The mutation beta3(Y747A) disrupted this reverse-turn tendency and markedly reduced the affinity of the head domain of the cytoskeletal protein, talin for the beta3 tail. Omission of the (Gly)(3) linker connecting the coiled-coiled helices and the integrin tails lead to helix propagation into the beta3 tail extending up to eight residues. A variety of different tail constructs were made and studied to reveal tail-tail interactions, but surprisingly no significant interactions between both tails could be detected within the context of our constructs. These results provide structural insight into a highly conserved beta tail motif (NPXY/F) required for integrin signaling and highlight a second transiently structured region (residues Arg(724)-Ala(735)), which might also be of functional significance.
NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin ?(1) ?(1).
NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin ?(1) ?(1).
NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin ?(1) ?(1).
Proteins. 2011 May 10;
Authors: Carbajo RJ, Sanz L, Mosulén S, Pérez A, Marcinkiewicz C, Pineda-Lucena A, Calvete JJ
NMR analysis of four recombinant jerdostatin molecules was assessed to define the structural basis of two naturally occurring gain-of-function events: C-terminal dipeptide processing and...
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06-10-2011 11:52 AM
The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study.
The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study.
The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study.
Structure. 2010 Oct 13;18(10):1280-8
Authors: Kalli AC, Wegener KL, Goult BT, Anthis NJ, Campbell ID, Sansom MS
Integrins are cell surface receptors crucial for cell migration and adhesion. They are activated by interactions of the talin head domain with the membrane surface and the integrin ? cytoplasmic tail. Here, we use coarse-grained molecular dynamic...
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03-03-2011 12:34 PM
NMR analysis of the αIIbβ3 cytoplasmic interaction suggests a mechanism for integrin regulation [Biochemistry]
NMR analysis of the αIIbβ3 cytoplasmic interaction suggests a mechanism for integrin regulation
Metcalf, D. G., Moore, D. T., Wu, Y., Kielec, J. M., Molnar, K., Valentine, K. G., Wand, A. J., Bennett, J. S., DeGrado, W. F....
Date: 2010-12-28
The integrin ?IIb?3 is a transmembrane (TM) heterodimeric adhesion receptor that exists in equilibrium between resting and active ligand binding conformations. In resting ?IIb?3, the TM and cytoplasmic domains of ?IIb and ?3 form a heterodimer that constrains ?IIb?3 in its resting conformation. To study the structure and dynamics of...
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01-03-2011 10:48 PM
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation [Biochemistry]
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation
Metcalf, D. G., Moore, D. T., Wu, Y., Kielec, J. M., Molnar, K., Valentine, K. G., Wand, A. J., Bennett, J. S., DeGrado, W. F....
Date: 2010-12-28
The integrin IIbβ3 is a transmembrane (TM) heterodimeric adhesion receptor that exists in equilibrium between resting and active ligand binding conformations. In resting IIbβ3, the TM and cytoplasmic domains of IIb and β3 form a heterodimer that constrains IIbβ3 in its resting conformation. To study the structure...
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12-29-2010 06:01 AM
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation.
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation.
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation.
Proc Natl Acad Sci U S A. 2010 Dec 14;
Authors: Metcalf DG, Moore DT, Wu Y, Kielec JM, Molnar K, Valentine KG, Wand AJ, Bennett JS, Degrado WF
The integrin ?IIb?3 is a transmembrane (TM) heterodimeric adhesion receptor that exists in equilibrium between resting and active ligand binding conformations. In resting ?IIb?3, the TM and...
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12-16-2010 09:21 PM
[NMR paper] Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through
Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50.
Related Articles Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50.
J Biol Chem. 1998 Oct 16;273(42):27357-63
Authors: McInnes C, Wang J, Al Moustafa AE, Yansouni C, O'Connor-McCourt M, Sykes BD
The investigation of a...
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11-17-2010 11:15 PM
[NMR paper] Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumi
Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study.
Related Articles Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study.
Biochemistry. 1993 Feb 23;32(7):1707-18
Authors: Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM
Two-dimensional 1H-NMR spectroscopy has been used to study the acid-denatured molten globule (A-state) of alpha-lactalbumin. The NMR spectra show that chemical shift dispersion is limited...
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08-21-2010 11:53 PM
Paramagnetic tagging for protein structure and dynamics analysis
Paramagnetic tagging for protein structure and dynamics analysis
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 12 August 2010</br>
Peter H.J., Keizers , Marcellus, Ubbink</br>
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NMR analysis of structure and dynamics of the cytosolic tails of integrin alpha IIb b
Linear Mode
