title: Structure of filamin A immunoglobulin-like repeat 10 from Homo sapiens.
abstract: Filamin A (FlnA) plays a critical role in cytoskeletal organization, cell motility and cellular signaling. FlnA utilizes different binding sites on a series of 24 immunoglobulin-like domains (Ig repeats) to interact with diverse cytosolic proteins and with cytoplasmic portions of membrane proteins. Mutations in a specific domain, Ig10 (FlnA-Ig10), are correlated with two severe forms of the otopalatodigital syndrome spectrum disorders Melnick-Needles syndrome and frontometaphyseal dysplasia. The crystal structure of FlnA-Ig10 determined at 2.44 Å resolution provides insight into the perturbations caused by these mutations.
authors.affiliation: Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA. pager2@ccf.org
authors.forename: Richard C
authors.initials: RC
authors.lastname: Page
authors.forename: Jeffrey G
authors.initials: JG
authors.lastname: Clark
authors.forename: Saurav
authors.initials: S
authors.lastname: Misra
mesh_terms: D003285:Contractile Proteins / Q000737:chemistry* / Q000235:genetics; D064448:Filamins; D006801:Humans; D007136:Immunoglobulins / Q000737:chemistry; D008840:Microfilament Proteins / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D009154:Mutation; D017434:Protein Structure, Tertiary; D020449:Repetitive Sequences, Amino Acid
chemical_list: D003285:Contractile Proteins; D064448:Filamins; D007136:Immunoglobulins; D008840:Microfilament Proteins