1a7x
From Proteopedia
FKBP12-FK1012 COMPLEX
Structural highlights
FunctionFKB1A_HUMAN Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA ligand that simultaneously binds two proteins must have two high affinity protein binding domains joined in a fashion that facilitates, or at least does not prevent, protein-protein interaction. Designing such ligands is challenging, and a high resolution X-ray structure of FKBP12-FK1012A-FKBP12 illustrates the subtleties of one successful design. Chemical inducers of dimerization: the atomic structure of FKBP12-FK1012A-FKBP12.,Schultz LW, Clardy J Bioorg Med Chem Lett. 1998 Jan 6;8(1):1-6. PMID:9871618[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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