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Blood, 1 March 2006, Vol. 107, No. 5, pp. 1925-1932.
Prepublished online as a Blood First Edition Paper on November 17, 2005; DOI 10.1182/blood-2005-10-3964.
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HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
The structure of the GPIb–filamin A complex
Fumihiko Nakamura,
Regina Pudas,
Outi Heikkinen,
Perttu Permi,
Ilkka Kilpeläinen,
Adam D. Munday,
John H. Hartwig,
Thomas P. Stossel, and
Jari Ylänne
From the Hematology Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA; Biocenter Oulu and Department of Biochemistry, University of Oulu, Finland; Laboratory of Organic Chemistry, Department of Chemistry, and Institute of Biotechnology, University of Helsinki, Finland; Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia; and Department of Biological and Environmental Science, University of Jyväskylä, Finland.
Filamin A (FLNa), a dimeric actin cross-linking and scaffold protein with numerous intracellular binding partners, anchors the platelet adhesion glycoprotein (GP) Ib-IX-V receptor to actin cytoskeleton. We mapped the GPIb binding site to a single domain of FLNa and resolved the structure of this domain and its interaction complex with the corresponding GPIb cytoplasmic domain. This is the first atomic structure of this class of membrane glycoprotein–cytoskeleton connection. GPIb binds in a groove formed between the C and D  strands of FLNa domain 17. The interaction is strikingly similar to that between the 7 integrin tail and a different FLNa domain, potentially defining a conserved motif for FLNa binding. Nevertheless, the structures also reveal specificity of the interfaces, which explains different regulatory mechanisms. To verify the topology of GPIb-FLNa interaction we also purified the native complex from platelets and showed that GPIb interacts with the C-terminus of FLNa, which is in accordance with our biochemical and structural data.
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