Related ArticlesNMR Structure, Dynamics and Interactions of the Integrin ?2 Cytoplasmic Tail with Filamin Domain IgFLNa21.
Sci Rep. 2018 Apr 03;8(1):5490
Authors: Chatterjee D, Zhiping LL, Tan SM, Bhattacharjya S
Abstract
Integrins are transmembrane proteins that mediate cell adhesion and migration. Each integrin is a heterodimer formed by an ? and a ? subunit. A large number of cytoplasmic proteins interact with the cytoplasmic tails (CTs) of integrins. The actin-binding cytoskeletal protein filamin A is a negative regulator of integrin activation. The IgFLNa21 domain of filamin A binds to the C-terminus of ?2 CT that contains a TTT-motif. Based on x-ray crystallography, it has been reported that the integrin ?2 CT forms a ? strand that docks into the ? strands C and D of IgFLNa21. In this study, we performed solution NMR analyses of IgFLNa21 in the presence of integrin ?2 CT peptides, and hybrid IgFLNa21, a construct of covalently linked IgFLNa21 and ?2 CT. The atomic resolution structure of the hybrid IgFLNa21 demonstrated conserved binding mode with ?2 CT. Although, 15N relaxation, model free analyses and H-D exchange studies have uncovered important insights into the conformational dynamics and stability of ?2 CT in complex with IgFLNa21. Such dynamical characteristics are likely to be necessary for the TTT-motif to serve as a phosphorylation switch that regulates filamin A binding to integrin ?2 CT.
[NMR paper] NMR Structure of Integrin ?4 Cytosolic Tail and Its Interactions with Paxillin.
NMR Structure of Integrin ?4 Cytosolic Tail and Its Interactions with Paxillin.
Related Articles NMR Structure of Integrin ?4 Cytosolic Tail and Its Interactions with Paxillin.
PLoS One. 2013;8(1):e55184
Authors: Chua GL, Patra AT, Tan SM, Bhattacharjya S
Abstract
BACKGROUND: Integrins are a group of transmembrane signaling proteins that are important in biological processes such as cell adhesion, proliferation and migration. Integrins are ?/? hetero-dimers and there are 24 different integrins formed by specific combinations of 18 ? and 8...
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02-06-2013 10:18 PM
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
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] NMR analysis of structure and dynamics of the cytosolic tails of integrin alpha IIb b
NMR analysis of structure and dynamics of the cytosolic tails of integrin alpha IIb beta 3 in aqueous solution.
Related Articles NMR 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...
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11-19-2010 08:32 PM
[NMR paper] Conformation of the cytoplasmic domain of phospholamban by NMR and CD.
Conformation of the cytoplasmic domain of phospholamban by NMR and CD.
Related Articles Conformation of the cytoplasmic domain of phospholamban by NMR and CD.
Mol Membr Biol. 1994 Oct-Dec;11(4):263-9
Authors: Hubbard JA, MacLachlan LK, Meenan E, Salter CJ, Reid DG, Lahouratate P, Humphries J, Stevens N, Bell D, Neville WA
Nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy have been used to characterize the conformation of the putative cytoplasmic domain of phospholamban (PLB), an oligomeric membrane-bound protein which...
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08-22-2010 03:29 AM
[KPWU blog] [IDP] Cytoplasmic Domain of the T Cell Receptor zeta
Cytoplasmic Domain of the T Cell Receptor zeta
Title:* The Intrinsically Disordered Cytoplasmic Domain of the T Cell Receptor ? Chain Binds to the Nef Protein of Simian Immunodeficiency Virus without a Disorder-to-Order Transition Authors: Alexander B. Sigalov, Walter M. Kim, Maria Saline and Lawrence J. Stern Journal: Biochemistry, 2008, 47 (49), pp 12942–12944 Not fully labeled in HSQChttp://stats.wordpress.com/b.gif?host=kpwu.wordpress.com&blog=76132&post=197&subd=kpwu&ref=&feed=1
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