ArticleProtein science : a publication of the Protein Society2005
The crystal structure of calcium- and integrin-binding protein 1: insights into redox regulated functions.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 36 citations in OpenAlex.
- AlphaFold2-Based Characterization of Apo and Holo Protein Structures and Conformational Ensembles Using Randomized Alanine Sequence Scanning Adaptation: Capturing Shared Signature Dynamics and Ligand-Induced Conformational Changes.International journal of molecular sciences · 2024Article
- Small-Molecule Disruptors of the Interaction between Calcium- and Integrin-Binding Protein 1 and Integrin αACS pharmacology & translational science · 2024Article
- Toward physics-based precision medicine: Exploiting protein dynamics to design new therapeutics and interpret variants.Protein science : a publication of the Protein Society · 2024Review
- Identification of Covalent Cyclic Peptide Inhibitors in mRNA Display.Journal of the American Chemical Society · 2023Article
- Predicting locations of cryptic pockets from single protein structures using the PocketMiner graph neural network.Nature communications · 2023Article
- Calcium- and Integrin-Binding Protein 2 (CIB2) in Physiology and Disease: Bright and Dark Sides.International journal of molecular sciences · 2022Review
- Discovery and Development of Cyclic Peptide Inhibitors of CIB1.ACS medicinal chemistry letters · 2021Article
- CIB4 is essential for the haploid phase of spermatogenesis in mice†.Biology of reproduction · 2020Article
- 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
- Evolutionary Conserved Positions Define Protein Conformational Diversity.PLoS computational biology · 2016Article
- The Landscape of Intertwined Associations in Homooligomeric Proteins.Biophysical journal · 2015Review
- MetalS(3), a database-mining tool for the identification of structurally similar metal sites.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Contra-regulation of calcium- and integrin-binding protein 1-induced cell migration on fibronectin by PAK1 and MAP kinase signaling.Journal of cellular biochemistry · 2011Article
- Nuclear magnetic resonance structure of calcium-binding protein 1 in a Ca(2+) -bound closed state: implications for target recognition.Protein science : a publication of the Protein Society · 2011Article
- Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions with the platelet integrin alphaIIb cytoplasmic domain.The Journal of biological chemistry · 2011Article
- Auxiliary Ca2+ binding sites can influence the structure of CIB1.Protein science : a publication of the Protein Society · 2009Article
- The purification, crystallization and preliminary diffraction of a glycerophosphodiesterase from Enterobacter aerogenes.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Calcium- and integrin-binding protein 1 (CIB1) is involved in the process of platelet aggregation by binding the cytoplasmic tail of the alpha(IIb) subunit of the platelet-specific integrin alpha(Iib)beta(3). Although poorly understood, it is widely believed that CIB1 acts as a global signaling regulator because it is expressed in many tissues that do not express integrin alpha(Iib)beta(3). We report the structure of human CIB1 to a resolution of 2.3 A, crystallized as a dimer. The dimer interface includes an extensive hydrophobic patch in a crystal form with 80% solvent content. Although the dimer form of CIB1 may not be physiologically relevant, this intersub-unit surface is likely to be linked to alpha(IIb) binding and to the binding of other signaling partner proteins. The C-terminal domain of CIB1 is structurally similar to other EF-hand proteins such as calmodulin and calcineurin B. Despite structural homology to the C-terminal domain, the N-terminal domain of CIB1 lacks calcium-binding sites. The structure of CIB1 revealed a complex with a molecule of glutathione in the reduced state bond to the N-terminal domain of one of the two subunits poised to interact with the free thiol of C35. Glutathione bound in this fashion suggests CIB1 may be redox regulated. Next to the bound GSH, the orientation of residues C35, H31, and S48 is suggestive of a cysteine-type protein phosphatase active site. The potential enzymatic activity of CIB1 is discussed and suggests a mechanism by which it regulates a wide variety of proteins in cells in addition to platelets.
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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.