ArticleJournal of the American Chemical Society2012
Structural basis for the activation of platelet integrin αIIbβ3 by calcium- and integrin-binding protein 1.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- The Diverse Functions of the Calcium- and Integrin-Binding Protein Family.International journal of molecular sciences · 2025Review
- Small-Molecule Disruptors of the Interaction between Calcium- and Integrin-Binding Protein 1 and Integrin αACS pharmacology & translational science · 2024Article
- The SIRT3-ATAD3A axis regulates MAM dynamics and mitochondrial calcium homeostasis in cardiac hypertrophy.International journal of biological sciences · 2024Article
- Discovery and Development of Cyclic Peptide Inhibitors of CIB1.ACS medicinal chemistry letters · 2021Article
- An Integrative Approach to Determine 3D Protein Structures Using Sparse Paramagnetic NMR Data and Physical Modeling.Frontiers in molecular biosciences · 2021Article
- Discovery and Characterization of Peptide Inhibitors for Calcium and Integrin Binding Protein 1.ACS chemical biology · 2020Article
- Molecular analysis of CIB4 gene and protein in Kermani sheep.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2017Article
- CIB1: a small protein with big ambitions.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Review
- Novel and recurrent CIB2 variants, associated with nonsyndromic deafness, do not affect calcium buffering and localization in hair cells.European journal of human genetics : EJHG · 2016Article
- αIIbβ3: structure and function.Journal of thrombosis and haemostasis : JTH · 2015Review
- The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB.The Journal of biological chemistry · 2014Article
- Role of the two structural domains from the periplasmic Escherichia coli histidine-binding protein HisJ.The Journal of biological chemistry · 2013Article
- Identification of novel integrin binding partners for calcium and integrin binding protein 1 (CIB1): structural and thermodynamic basis of CIB1 promiscuity.Biochemistry · 2013Article
- Alterations of the CIB2 calcium- and integrin-binding protein cause Usher syndrome type 1J and nonsyndromic deafness DFNB48.Nature genetics · 2012Article
- Structural insights into calmodulin-regulated L-selectin ectodomain shedding.The Journal of biological chemistry · 2012Article
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Calcium and integrin binding protein 1 (CIB1) is a specific binding partner for the cytoplasmic domain of the αIIb subunit of the highly abundant platelet integrin αIIbβ3. This protein has been suggested to be involved in the regulation of the activation of αIIbβ3, a process leading to platelet aggregation and blood coagulation. In this work, the solution structure of the deuterated Ca(2+)-CIB1 protein complexed with an αIIb peptide was first determined through modern RDC-based NMR methods. Next, we generated a complex structure for CIB1 and the αIIb domain (Ca(2+)-CIB1/αIIb) using the program Haddock, which is based on experimental restraints obtained for the protein-peptide interface from cross-saturation NMR experiments. In this data-driven complex structure, the N-terminal α-helix of the cytoplasmic domain of αIIb is buried in the hydrophobic pocket of the C-lobe of Ca(2+)-CIB1. The C-terminal acidic tail of αIIb remains unstructured and likely interacts with several positively charged residues in the N-lobe of Ca(2+)-CIB1. A potential molecular mechanism for the CIB1-mediated activation of the platelet integrin could be proposed on the basis of the model structure of this protein complex. Another feature of this work is that, in the NMR cross-saturation experiments, we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1 through its selectively protonated methyl groups. This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
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Registered trials
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.