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      Structure and dynamics of the platelet integrin-binding C4 domain of von Willebrand factor

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          Key Points

          The high-resolution structure and associated dynamics of the platelet integrin-binding VWF C4 domain is presented. A possible mechanism of gain-of-function variant affecting the arrangement with neighboring domains is proposed.

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          Most cited references38

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          Modified Spin-Echo Method for Measuring Nuclear Relaxation Times

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            Is Open Access

            SMART: recent updates, new developments and status in 2015

            SMART (Simple Modular Architecture Research Tool) is a web resource (http://smart.embl.de/) providing simple identification and extensive annotation of protein domains and the exploration of protein domain architectures. In the current version, SMART contains manually curated models for more than 1200 protein domains, with ∼200 new models since our last update article. The underlying protein databases were synchronized with UniProt, Ensembl and STRING, bringing the total number of annotated domains and other protein features above 100 million. SMART's ‘Genomic’ mode, which annotates proteins from completely sequenced genomes was greatly expanded and now includes 2031 species, compared to 1133 in the previous release. SMART analysis results pages have been completely redesigned and include links to several new information sources. A new, vector-based display engine has been developed for protein schematics in SMART, which can also be exported as high-resolution bitmap images for easy inclusion into other documents. Taxonomic tree displays in SMART have been significantly improved, and can be easily navigated using the integrated search engine.
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              Biochemistry and genetics of von Willebrand factor.

              J Sadler (1998)
              Von Willebrand factor (VWF) is a blood glycoprotein that is required for normal hemostasis, and deficiency of VWF, or von Willebrand disease (VWD), is the most common inherited bleeding disorder. VWF mediates the adhesion of platelets to sites of vascular damage by binding to specific platelet membrane glycoproteins and to constituents of exposed connective tissue. These activities appear to be regulated by allosteric mechanisms and possibly by hydrodynamic shear forces. VWF also is a carrier protein for blood clotting factor VIII, and this interaction is required for normal factor VIII survival in the circulation. VWF is assembled from identical approximately 250 kDa subunits into disulfide-linked multimers that may be > 20,000 kDa. Mutations in VWD can disrupt this complex biosynthetic process at several steps to impair the assembly, intracellular targeting, or secretion of VWF multimers. Other VWD mutations impair the survival of VWF in plasma or the function of specific ligand binding sites. This growing body of information about VWF synthesis, structure, and function has allowed the reclassification of VWD based upon distinct pathophysiologic mechanisms that appear to correlate with clinical symptoms and the response to therapy.
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                Author and article information

                Journal
                Blood
                American Society of Hematology
                0006-4971
                1528-0020
                January 24 2019
                January 24 2019
                : 133
                : 4
                : 366-376
                Affiliations
                [1 ]Hamburg Unit, European Molecular Biology Laboratory, Hamburg, Germany;
                [2 ]Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany;
                [3 ]INSERM, UMR_S 1176, Université Paris-Sud, Université Paris-Saclay, Le Kremlin-Bicêtre, France;
                [4 ]Heidelberg Institute for Theoretical Studies, Heidelberg, Germany;
                [5 ]Interdisciplinary Center for Scientific Computing, Mathematikon, Heidelberg University, Heidelberg, Germany;
                [6 ]Max Planck Tandem Group in Computational Biophysics, University of Los Andes, Bogotá, Colombia;
                [7 ]Department of Pediatric Hematology and Oncology, University Medical Centre Hamburg-Eppendorf, Hamburg, Germany; and
                [8 ]University Medical Centre Hamburg-Eppendorf, Hamburg, Germany
                Article
                10.1182/blood-2018-04-843615
                6450055
                30305279
                e4eca0a5-a731-45c3-9f98-97c4a86f93f3
                © 2019
                History

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