3RGH
Structure of filamin A immunoglobulin-like repeat 10 from Homo sapiens
Summary for 3RGH
| Entry DOI | 10.2210/pdb3rgh/pdb |
| Related | 2DIA |
| Descriptor | Filamin-A, ACETATE ION (3 entities in total) |
| Functional Keywords | cell adhesion, cytoskeleton-complex, disease mutation, immunoglobulin like, filamin, cytoskeleton, actin-binding, cell junction, cell shape, immunoglobulin-like beta-sandwich, cd4, beta-mercaptoethanol adduct |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm, cell cortex: P21333 |
| Total number of polymer chains | 2 |
| Total formula weight | 21001.41 |
| Authors | Page, R.C.,Clark, J.,Misra, S. (deposition date: 2011-04-08, release date: 2011-08-03, Last modification date: 2024-11-20) |
| Primary citation | Page, R.C.,Clark, J.G.,Misra, S. Structure of filamin A immunoglobulin-like repeat 10 from Homo sapiens. Acta Crystallogr.,Sect.F, 67:871-876, 2011 Cited by PubMed 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. PubMed: 21821884DOI: 10.1107/S1744309111024249 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.44 Å) |
Structure validation
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