2aqz

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spinqualitylabelsall models 2aqz, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of FGF-1, S17T/N18T/G19 deletion mutant

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Human acidic fibroblast growth factor (FGF-1) is a member of the, beta-trefoil superfold, a protein architecture that exhibits a, characteristic threefold axis of structural symmetry. FGF-1 contains 11, beta-turns, the majority being type I 3:5; however, a type I 4:6 turn is, also found at three symmetry-related locations. The relative uniqueness of, the type I 4:6 turn in the FGF-1 structure suggests it may play a key role, in the stability, folding, or function of the protein. To test this, hypothesis a series of deletion mutations were constructed, the aim of, which was to convert existing type I 4:6 turns at two locations into type, I 3:5 turns. The results show it is possible to successfully substitute, the type I 4:6 turn by a type I 3:5 turn with minimal impact upon protein, stability or folding. Thus, these different turn structures, even though, they differ in length, exhibit similar energetic properties. Additional, sequence swapping mutations within the introduced type I 3:5 turns, suggests that the turn sequence primarily affects stability but not turn, structure (which appears dictated primarily by the local environment)., Although the results suggest that a stable, foldable beta-trefoil protein, may be designed utilizing a single turn type (type I 3:5), a type I 4:6, turn at turn 1 of FGF-1 appears essential for efficient mitogenic, function.

Disease

Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[602115], LADD syndrome OMIM:[602115]

About this Structure

2AQZ is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

Conversion of type I 4:6 to 3:5 beta-turn types in human acidic fibroblast growth factor: effects upon structure, stability, folding, and mitogenic function., Lee J, Dubey VK, Somasundaram T, Blaber M, Proteins. 2006 Mar 15;62(3):686-97. PMID:16355415

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