RiAFP

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The asymmetric unit comprises two RiAFP molecules juxtaposed with their ice-binding surfaces, however the protein is monomer in the solutio

Overall Structure

The crystallographic structure of RiAFP was defined recently^[3]. It reveals a new β-solenoid architecture that forms of of remarkable regularity. The β-sheets lie on top of each other with the upper and lower strands parallel but in the opposite orientation. Two ends deviate from β helix regularity by forming . These capping structures help to prevent end-to-end associations that would spoil the solubility of RiAFP and lead to oligomerization and aggregation.

Function

Disease

Relevance

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. The three residues in �-strand 11 at the C terminus that are too bulky to be accommodated into the core may also contribute to the capping structure to prevent amyloid-like polymerization.

Within the core there are between Thr-Ser (65-55, 85-75, 132-124 respectively) and one between Cys4-Cys21, that contributes to stabilize the whole structure.