2lhe

Gb98-T25I,L20A

spinqualitylabelsall models 2lhe Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lhe is a 1 chain structure with sequence from Synthetic construct. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed While disordered to ordered rearrangements are relatively common, the ability of proteins to switch from one ordered fold to a completely different fold is generally regarded as rare, and few fold switches have been characterized. Here, in a designed system, we examine the mutational requirements for transitioning between folds and functions. We show that switching between monomeric 3alpha and 4beta+alpha folds can occur in multiple ways with successive single amino acid changes at diverse residue positions, raising the likelihood that such transitions occur in the evolution of new folds. Even mutations on the periphery of the core can tip the balance between alternatively folded states. Ligand-binding studies illustrate that a new immunoglobulin G-binding function can be gained well before the relevant 4beta+alpha fold is appreciably populated in the unbound protein. The results provide new insights into the evolution of fold and function. Mutational tipping points for switching protein folds and functions.,He Y, Chen Y, Alexander PA, Bryan PN, Orban J Structure. 2012 Feb 8;20(2):283-91. PMID:22325777 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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