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-Structure paper
Title | Mutation in a flexible linker modulates binding affinity for modular complexes. |
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Journal, issue, pages | Proteins, Vol. 87, Issue 5, Page 425-429, Year 2019 |
Publish date | Mar 9, 2019 |
![]() | Philippa H Stokes / Neil O Robertson / Ana P G Silva / Tanya Estephan / Jill Trewhella / J Mitchell Guss / Jacqueline M Matthews / ![]() |
PubMed Abstract | Tandem beta zippers are modular complexes formed between repeated linear motifs and tandemly arrayed domains of partner proteins in which β-strands form upon binding. Studies of such complexes, ...Tandem beta zippers are modular complexes formed between repeated linear motifs and tandemly arrayed domains of partner proteins in which β-strands form upon binding. Studies of such complexes, formed by LIM domain proteins and linear motifs in their intrinsically disordered partners, revealed spacer regions between the linear motifs that are relatively flexible but may affect the overall orientation of the binding modules. We demonstrate that mutation of a solvent exposed side chain in the spacer region of an LHX4-ISL2 complex has no significant effect on the structure of the complex, but decreases binding affinity, apparently by increasing flexibility of the linker. |
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Methods | SAS (X-ray synchrotron) / X-ray diffraction |
Resolution | 1.92 Å |
Structure data | ![]() SASDDQ4: ![]() SASDDR4: ![]() PDB-6cme: |
Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-HOH: |
Source |
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![]() | TRANSCRIPTION / LIM-homeodomain / cell-type specification / neural development |