2l3p | pdb_00002l3p

Structure of the prolyl cis isomer of the Crk Protein

spinqualitylabelsall models 2l3p, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l3p is a 1 chain structure with sequence from Gallus gallus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2l3q, 2l3s Gene: CRK (Gallus gallus) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Proline switches, controlled by cis-trans isomerization, have emerged as a particularly effective regulatory mechanism in a wide range of biological processes. Here we report the structures of both the cis and trans conformers of a proline switch in the Crk signaling protein. Proline isomerization toggles Crk between two conformations: an autoinhibitory conformation, stabilized by the intramolecular association of two tandem SH3 domains in the cis form, and an uninhibited, activated conformation promoted by the trans form. In addition to acting as a structural switch, the heterogeneous proline recruits cyclophilin A, which accelerates the interconversion rate between the isomers, thereby regulating the kinetics of Crk activation. The data provide atomic insight into the mechanisms that underpin the functionality of this binary switch and elucidate its remarkable efficiency. The results also reveal new SH3 binding surfaces, highlighting the binding versatility and expanding the noncanonical ligand repertoire of this important signaling domain. Structural basis for regulation of the Crk signaling protein by a proline switch.,Sarkar P, Saleh T, Tzeng SR, Birge RB, Kalodimos CG Nat Chem Biol. 2011 Jan;7(1):51-7. Epub 2010 Dec 5. PMID:21131971 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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