2BP3

Crystal structure of Filamin A domain 17 and GPIb alpha cytoplasmic domain complex

Summary for 2BP3

• Entry DOI: 10.2210/pdb2bp3/pdb
• Related: 1GWB 1K13 1M0Z 1M10 1OOK 1P8V 1P9A 1QYY 1SQ0 2BRQ
• Descriptor: FILAMIN A, PLATELET GLYCOPROTEIN IB ALPHA CHAIN, GLYCEROL, ... (4 entities in total)
• Functional Keywords: structural protein, cytoskeleton-complex, actin binding protein, cytoskeleton, complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm, cell cortex: P21333; Membrane; Single-pass type I membrane protein: P07359
• Total number of polymer chains: 4
• Total formula weight: 25262.25

Authors

Pudas, R.,Ylanne, J. (deposition date: 2005-04-18, release date: 2005-11-30, Last modification date: 2023-12-13)

Primary citation

Nakamura, F.,Pudas, R.,Heikkinen, O.,Permi, P.,Kilpelainen, I.,Munday, A.D.,Hartwig, J.H.,Stossel, T.P.,Ylanne, J.
The Structure of the Gpib-Filamin a Complex.
Blood, 107:1925-, 2006

PubMed Abstract: 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 GPIbalpha binding site to a single domain of FLNa and resolved the structure of this domain and its interaction complex with the corresponding GPIbalpha cytoplasmic domain. This is the first atomic structure of this class of membrane glycoprotein-cytoskeleton connection. GPIbalpha binds in a groove formed between the C and D beta strands of FLNa domain 17. The interaction is strikingly similar to that between the beta7 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.

PubMed: 16293600
DOI: 10.1182/BLOOD-2005-10-3964

Experimental method

X-RAY DIFFRACTION (2.32 Å)