2W86

Crystal structure of fibrillin-1 domains cbEGF9hyb2cbEGF10, calcium saturated form

Summary for 2W86

• Entry DOI: 10.2210/pdb2w86/pdb
• Related: 1APJ 1LMJ 1UZJ 1UZK 1UZP 1UZQ
• Descriptor: FIBRILLIN-1, CALCIUM ION, IODIDE ION, ... (4 entities in total)
• Functional Keywords: fibrillin, phosphoprotein, egf-like domain, disease mutation, craniosynostosis, extracellular matrix, fibrillin calcium cbegf hybrid, calcium, secreted, polymorphism, glycoprotein
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Secreted, extracellular space, extracellular matrix: P35555
• Total number of polymer chains: 1
• Total formula weight: 15988.58

Authors

Jensen, S.A.,Iqbal, S.,Lowe, E.D.,Redfield, C.,Handford, P.A. (deposition date: 2009-01-09, release date: 2009-05-26, Last modification date: 2011-07-13)

Primary citation

Jensen, S.A.,Iqbal, S.,Lowe, E.D.,Redfield, C.,Handford, P.A.
Structure and Interdomain Interactions of a Hybrid Domain: A Disulphide-Rich Module of the Fibrillin/Ltbp Superfamily of Matrix Proteins.
Structure, 17:759-, 2009

PubMed Abstract: The fibrillins and latent transforming growth factor-beta binding proteins (LTBPs) form a superfamily of structurally-related proteins consisting of calcium-binding epidermal growth factor-like (cbEGF) domains interspersed with 8-cysteine-containing transforming growth factor beta-binding protein-like (TB) and hybrid (hyb) domains. Fibrillins are the major components of the extracellular 10-12 nm diameter microfibrils, which mediate a variety of cell-matrix interactions. Here we present the crystal structure of a fibrillin-1 cbEGF9-hyb2-cbEGF10 fragment, solved to 1.8 A resolution. The hybrid domain fold is similar, but not identical, to the TB domain fold seen in previous fibrillin-1 and LTBP-1 fragments. Pairwise interactions with neighboring cbEGF domains demonstrate extensive interfaces, with the hyb2-cbEGF10 interface dependent on Ca(2+) binding. These observations provide accurate constraints for models of fibrillin organization within the 10-12 nm microfibrils and provide further molecular insights into how Ca(2+) binding influences the intermolecular interactions and biomechanical properties of fibrillin-1.

PubMed: 19446531
DOI: 10.1016/J.STR.2009.03.014

Experimental method

X-RAY DIFFRACTION (1.8 Å)