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Fibrillin-1 (PDB ID: 2W86) is a protein which is encoded in human bodies by the gene FBN1 situated on chromosome 15. Fibrillin-1 is a single protein chain from the class of glycoproteins with a mass of 350 kDa and it forms microfibrils located in the extracellular matrix. Thus, fibrillin-1 has a role in the structural support of cells in elastic and nonelastic connective tissue in the human body.

Structure

The protein contains multiple subunits called epidermal growth factor (EGF) and transforming growth factor β binding protein-like domain (7 TGF-bp). EGF are repeated in tandem along the whole protein which represents about 75% of the total fibrillin-1 lenght and they are interrupted by the insertion of TGF-bp unit. In total, there are 47 motifs of EGF in one fibrillin-1, but only 43 of them contain calcium binding sequences. In consequence, these EGF are named cb-EGF for their ability to bind calcium cations (Proteopedia 3D visualization of two tandem cb-EGF). Each of EGF or cb-EGF unit contains 6 residues of cysteine which form 3 disulfide bridges (CYS1-CYS3,CYS2-CYS4,CYS5-CYS6)(Proteopedia 3D visualization of disulfide bridges) stabilizing the secondary structure of the protein. cb-EGF units contain also a Ca2+ binding site composed by aminoacids D,N,Q,E,Y and F which participate into the cation bonding and which can be seperated by different number of other aminoacids (D/N-x-D/N-E/Q-xm-D/N-xn-Y/F represents the binding site of Ca2+,x, xm, and xn represent certain number of amino acids). Amino acids which participate in the Ca2+ binding D, N, E, Q contain oxygen in their lateral chains and Y with F which contain an aromatic cycle. Oxygen atoms of D/N/Q/E are involved in the Ca2+ binding and create the binding site with the pentagonal bipyramidal geometry.

3D model represents these parts of fibrillin-1: , second hybrid domain and cb-EGF10.

Disease

Relevance

Structural highlights

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