The crystal structure of the tetrameric human vasohibin-1-SVBP complex reveals a variable arm region within the structural core.

ABSTRACT: Vasohibins regulate angiogenesis, tumor growth, metastasis and neuronal differentiation. They form a complex with small vasohibin-binding protein (SVBP) and show tubulin tyrosine carboxypeptidase activity. Recent crystal structure determinations of vasohibin-SVBP complexes have provided a molecular basis for complex formation, substrate binding and catalytic activity. However, the regulatory mechanism and dynamics of the complex remain elusive. Here, the crystal structure of the VASH1-SVBP complex and a molecular-dynamics simulation study are reported. The overall structure of the complex was similar to previously reported structures. Importantly, however, the structure revealed a domain-swapped heterotetramer that was formed between twofold symmetry-related molecules. This heterotetrameri

SUBMITTER: Ikeda A 

PROVIDER: S-EPMC7543661 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature