The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D

@article{Love2003TheLF,
  title={The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D},
  author={Christopher Anthony Love and Karl Harlos and Nasim Mavaddat and Simon J. Davis and David I. Stuart and E. Yvonne Jones and Robert Esnouf},
  journal={Nature Structural Biology},
  year={2003},
  volume={10},
  pages={843-848}
}
Semaphorins, proteins characterized by an extracellular sema domain, regulate axon guidance, immune function and angiogenesis. The crystal structure of SEMA4D (residues 1–657) shows the sema topology to be a seven-bladed β-propeller, revealing an unexpected homology with integrins. The sema β-propeller contains a distinctive 77-residue insertion between β-strands C and D of blade 5. Blade 7 is followed by a domain common to plexins, semaphorins and integrins (PSI domain), which forms a compact… 
Structure of Semaphorins and Their Receptors
TLDR
This chapter reviews the current knowledge of molecular architecture and interactions with the aim of identifying features and properties that fit the semaphorins and their receptors for biological function and delineates the limits of the understanding of molecular mechanism in semaphors.
The sema domain.
A Novel Adaptation of the Integrin PSI Domain Revealed from Its Crystal Structure*
TLDR
The crystal structure of PSI is reported in the context of the crystallized αVβ3 ectodomain and an unexpected feature of the structure is that the final, eighth cysteine is located C-terminal to the Ig-like hybrid domain and is thus separated by the hybrid domain from the other seven cysteines of PSi.
Structural basis for semaphorin signalling through the plexin receptor
TLDR
Homodimer-to-heterodimer transitions of cell-surface plexin that result in a specific orientation of its molecular axis relative to the membrane may constitute the structural mechanism by which the ligand-binding ‘signal’ is transmitted to the cytoplasmic region, inducing GAP domain rearrangements and activation.
Architecture of the Sema3A/PlexinA4/Neuropilin tripartite complex
TLDR
The cryo-EM structure of a near intact extracellular region complex of Sema3A, PlexinA4 and Neuropilin 1 (Nrp1) at 3.7 Å resolution is presented, suggesting an essential role for the long non-conserved linkers and the MAM domain in neuro pilin in the semaphorin/plexin/neuropil in complex.
Structural Basis of Semaphorin-Plexin Recognition and Viral Mimicry from Sema7A and A39R Complexes with PlexinC1
High-resolution structure of the catalytic region of MICAL (molecule interacting with CasL), a multidomain flavoenzyme-signaling molecule.
  • C. Siebold, N. Berrow, E. Jones
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 2005
TLDR
The 1.45-A resolution crystal structure of the FAD-containing MO domain of mouse MICAL-1, a multidomain cytosolic protein with a putative flavoprotein monooxygenase region required for semaphorin-plexin repulsive axon guidance, is reported.
Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
TLDR
The atomic basis for allosteric regulation of the conformation and affinity for ligand of the integrin ectodomain is defined, and how fibrinogen-mimetic therapeutics bind to platelet integrin αIIbβ3 is defined.
Transmembrane Recognition of the Semaphorin Co-Receptors Neuropilin 1 and Plexin A1: Coarse-Grained Simulations
TLDR
The role of the transmembrane domains of neuropilin 1 and plexin A1 for the dimerization of the two receptors is addressed by characterizing the assembly in lipid bilayers using coarse-grained molecular dynamics simulations and it is demonstrated that homodimerization and heterodimerizations are driven by GxxxG motifs.
Identification of a calmodulin-binding domain in Sema4D that regulates its exodomain shedding in platelets.
TLDR
The results show that the membrane-proximal cytoplasmic domain of Sema4D contains a binding site for calmodulin within the polybasic region Arg762-Lys779, and that dissociation of the complex is sufficient to trigger ADAM17-dependent cleavage of SemA4D, releasing a bioactive fragment.
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