9JU1: Helix-loop-helix peptide

Helix-loop-helix peptide (VS42-LR3) in complex with VEGF-A. Determined by X-ray diffraction at 1.45 Å resolution. Released 25 Dec 2024.

Method
X-ray diffraction
Resolution
1.45 Å
Organisms
synthetic construct, Homo sapiens
Chains
2
Atoms
1,281
Mol. weight
16.78 kDa
Released
25 Dec 2024

Explore 9JU1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9JU1 contains 5 α-helices and 7 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix13-164
α-helix17-248
β-strand2511
β-strand27-3482
α-helix35-384
β-strand46-4833
β-strand51-5882
β-strand6011
β-strand66-84193
β-strand88-106193
Chain C: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix2-1615
α-helix26-4217

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
VS42-LR3Cprotein44synthetic construct
Vascular endothelial growth factor A, long formAprotein102Homo sapiensP15692 (AlphaFold model)
Sequence of entity 1 (C), FASTA
>9JU1_1 VS42-LR3 (chains C)
CAAELAALEAELAALEGHVEEADFPWGKLNNLIEKLWQLKQACX
Sequence of entity 2 (A), FASTA
>9JU1_2 Vascular endothelial growth factor A, long form (chains A)
GQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLE
CVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKD

Primary citation

Structural insights into molecular-targeting helix-loop-helix peptide against vascular endothelial growth factor-A. Michigami, M., Notsu, K., Kamo, M. et al. Biochem Biophys Res Commun (2024) 734:150749. DOI 10.1016/j.bbrc.2024.150749 · PubMed

Other PDB entries of the same protein (UniProt P15692 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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