ArticleProceedings of the National Academy of Sciences of the United States of America2002
Solution structures of the cytoplasmic tail complex from platelet integrin alpha IIb- and beta 3-subunits.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
35 citing papers in PubMed, 100 citations in OpenAlex.
- Family-wide analysis of integrin structures predicted by AlphaFold2.bioRxiv : the preprint server for biology · 2023Article
- Family-wide analysis of integrin structures predicted by AlphaFold2.Computational and structural biotechnology journal · 2023Article
- Kindlin Assists Talin to Promote Integrin Activation.Biophysical journal · 2020Article
- Differential Binding of Active and Inactive Integrin to Talin.The protein journal · 2018Article
- On the contributing role of the transmembrane domain for subunit-specific sensitivity of integrin activation.Scientific reports · 2018Article
- A Conserved Ectodomain-Transmembrane Domain Linker Motif Tunes the Allosteric Regulation of Cell Surface Receptors.The Journal of biological chemistry · 2016Article
- Integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.PloS one · 2013Article
- Article
- Structural basis for the activation of platelet integrin αIIbβ3 by calcium- and integrin-binding protein 1.Journal of the American Chemical Society · 2012Article
- Integrin structure, activation, and interactions.Cold Spring Harbor perspectives in biology · 2011Review
- Transmembrane communication: general principles and lessons from the structure and function of the M2 proton channel, K⁺ channels, and integrin receptors.Annual review of biochemistry · 2011Review
- NMR analysis of the alphaIIb beta3 cytoplasmic interaction suggests a mechanism for integrin regulation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- A view into the blind spot: solution NMR provides new insights into signal transduction across the lipid bilayer.Structure (London, England : 1993) · 2010Review
- Structural diversity in integrin/talin interactions.Structure (London, England : 1993) · 2010Article
- Integrins as therapeutic targets: lessons and opportunities.Nature reviews. Drug discovery · 2010Review
- Ways and means of coping with uncertainties of the relationship of the genetic blue print to protein structure and function in the cell.Cell communication and signaling : CCS · 2010Article
- The final steps of integrin activation: the end game.Nature reviews. Molecular cell biology · 2010Review
- Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Multiple approaches converge on the structure of the integrin alphaIIb/beta3 transmembrane heterodimer.Journal of molecular biology · 2009Article
- Kindling the flame of integrin activation and function with kindlins.Current opinion in hematology · 2009Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integrin adhesion receptors constitute a cell-signaling system whereby interactions in the small cytoplasmic domains of the heterodimeric alpha- and beta-subunits provoke major functional alterations in the large extracellular domains. With two-dimensional NMR spectroscopy, we examined two synthetic peptides [alphaIIb((987)MWKVGFFKRNR) and beta3((716)KLLITIHDRKEFAKFEEERARAKWD)] encompassing the membrane-proximal regions of the cytoplasmic domain motifs from the platelet integrin complex alphaIotaIotabbeta3. These membrane-proximal regions contain two conserved motifs, represented by (989)KVGFFKR in the alphaIIb-subunit, and (716)KLLITIHDR in the beta3-subunit. The dimer interaction consists of two adjacent helices with residues V990 and F993 of the alphaIotaIotab-subunit heavily implicated in the dimer interfacial region, as is I719 of beta3. These residues are situated within the conserved motifs of their respective proteins. Further structural analysis of this unique peptide heterodimer suggests that two distinct conformers are present. The major structural difference between the two conformers is a bend in the beta3-peptide between D723 and A728, whereas the helical character in the other regions remains intact. Earlier mutational analysis has shown that a salt bridge between the side chains of alphaIotaIotab(R955) and beta3(D723) is formed. When this ion pair was modeled into both conformers, increased nuclear Overhauser effect violations suggested that the more bent structure was less able to accommodate this interaction. These results provide a molecular level rationalization for previously reported biochemical studies, as well as a basis for an atomic level understanding of the intermolecular interactions that regulate integrin activity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.