2N54: Disulfide stabilized XCL1 dimer

Solution structure of a disulfide stabilized XCL1 dimer. Determined by solution NMR. Released 7 Oct 2015.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 1,040
Mol. weight: 20.7 kDa
Released: 7 Oct 2015

Explore 2N54 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2N54 contains 2 α-helices and 8 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: 1 helix, 4 β-strands

Element	Residues	Length	Sheet
β-strand	12-14	3	1
α-helix	19-21	3
β-strand	25-31	7	1
β-strand	34-41	8	1
β-strand	44-50	7	1

Chain B: 1 helix, 4 β-strands

Element	Residues	Length	Sheet
β-strand	211-214	4	2
β-strand	225-231	7	2
β-strand	234-241	8	2
β-strand	244-250	7	2
α-helix	263-265	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Lymphotactin	A, B	protein	93	Homo sapiens	P47992 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2N54_1 Lymphotactin (chains A, B)
VGSEVSDKRTCVSLTTQRLPVSRIKTYTITEGSLRCVIFITKRGLKVCCDPQATWVRDVV
RSMDRKSNTRNNMIQTKPTGTQQSTNTAVTLTG

Primary citation

Engineering Metamorphic Chemokine Lymphotactin/XCL1 into the GAG-Binding, HIV-Inhibitory Dimer Conformation. Fox, J.C., Tyler, R.C., Guzzo, C. et al. ACS Chem Biol (2015) 10:2580-2588. DOI 10.1021/acschembio.5b00542 · PubMed

Other PDB entries of the same protein (UniProt P47992 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2NYZ 2.6 Å, Viral Chemokine Binding Protein M3 From Murine Gammaherpesvirus68 In Complex With The C-…
9AST 3.07 Å, Cryo-EM structure of XCR1 signaling complex
1J8I Solution Structure of Human Lymphotactin
1J9O Solution structure of human lymphotactin
2HDM Solution structure of V21C/V59C Lymphotactin/XCL1
2JP1 Solution structure of the alternative conformation of XCL1/Lymphotactin

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