6CME

Structure of wild-type ISL2-LID in complex with LHX4-LIM1+2

Summary for 6CME

• Entry DOI: 10.2210/pdb6cme/pdb
• Related: 2JTN 2rgt 3mmk
• Descriptor: LIM/homeobox protein Lhx4,Insulin gene enhancer protein ISL-2, ZINC ION (3 entities in total)
• Functional Keywords: lim-homeodomain, cell-type specification, neural development, transcription
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 2
• Total formula weight: 38022.08

Authors

Stokes, P.H.,Silva, A.,Guss, J.M.,Matthews, J.M. (deposition date: 2018-03-04, release date: 2019-04-10, Last modification date: 2023-10-04)

Primary citation

Stokes, P.H.,Robertson, N.O.,Silva, A.P.G.,Estephan, T.,Trewhella, J.,Guss, J.M.,Matthews, J.M.
Mutation in a flexible linker modulates binding affinity for modular complexes.
Proteins, 87:425-429, 2019

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, 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.

PubMed: 30788856
DOI: 10.1002/prot.25675

Experimental method

X-RAY DIFFRACTION (1.92 Å)