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TitleMutation in a flexible linker modulates binding affinity for modular complexes.
Journal, issue, pagesProteins, Vol. 87, Issue 5, Page 425-429, Year 2019
Publish dateMar 9, 2019
AuthorsPhilippa H Stokes / Neil O Robertson / Ana P G Silva / Tanya Estephan / Jill Trewhella / J Mitchell Guss / Jacqueline M Matthews /
PubMed AbstractTandem 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.
External linksProteins / PubMed:30788856
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution1.92 Å
Structure data

SASDDQ4:
LIM/homeobox protein Lhx4 LIM domains fused to the LIM interaction domain (LID) of Insulin gene enhancer protein ISL-2
Method: SAXS/SANS

SASDDR4:
LIM/homeobox protein Lhx4 LIM domains fused to the LIM interaction domain (LID) R282G mutant of Insulin gene enhancer protein ISL-2
Method: SAXS/SANS

PDB-6cme:
Structure of wild-type ISL2-LID in complex with LHX4-LIM1+2
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
KeywordsTRANSCRIPTION / LIM-homeodomain / cell-type specification / neural development

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