Figure 1
From: A human β-III-spectrin spinocerebellar ataxia type 5 mutation causes high-affinity F-actin binding
Leucine 253 is located in the E-F loop of the β-III-spectrin CH2 domain.
A structural homology model generated for the β-III-spectrin ABD (CH1 and CH2 domains, amino acids 56 to 284) is shown in green. The side-chain of β-III-spectrin leucine 253 is colored magenta. The crystal structure of the β-II-spectrin CH2 domain (PDB ID: 1BKR) is shown in grey and is aligned with the β-III-spectrin homology model. β-II-spectrin leucine 250 is the equivalent residue of β-III-spectrin leucine 253. The side-chain of β-II-spectrin leucine 250 is colored cyan. β-III-spectrin leucine 253 is in a loop connecting alpha-helices E and F of the CH2 domain. The side-chain of β-III-spectrin leucine 253 is in close position to CH2 domain alpha-helix G and CH1 domain alpha-helix A.
