3o3q | pdb_00003o3q
Crystal structure of "L44F/M67I/L73V/A103G/deletion 104-106/F108Y/V109L/L111I/C117V/R119G/deletion 120-122" mutant form of Human acidic fibroblast growth factor
Structural highlights
FunctionFGF1_HUMAN Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro.[1] [2] [3] Publication Abstract from PubMedFibroblast growth factor-1, a member of the 3-fold symmetric beta-trefoil fold, was subjected to a series of symmetric constraint mutations in a process termed "top-down symmetric deconstruction." The mutations enforced a cumulative exact 3-fold symmetry upon symmetrically equivalent positions within the protein and were combined with a stability screen. This process culminated in a beta-trefoil protein with exact 3-fold primary-structure symmetry that exhibited excellent folding and stability properties. Subsequent fragmentation of the repeating primary-structure motif yielded a 42-residue polypeptide capable of spontaneous assembly as a homotrimer, producing a thermostable beta-trefoil architecture. The results show that despite pronounced reduction in sequence complexity, pure symmetry in the design of a foldable, thermostable beta-trefoil fold is possible. The top-down symmetric deconstruction approach provides a novel alternative means to successfully identify a useful polypeptide "building block" for subsequent "bottom-up" de novo design of target protein architecture. A polypeptide "building block" for the beta-trefoil fold identified by "top-down symmetric deconstruction".,Lee J, Blaber SI, Dubey VK, Blaber M J Mol Biol. 2011 Apr 15;407(5):744-63. Epub 2011 Feb 16. PMID:21315087[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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