1HRJ

HUMAN RANTES, NMR, 13 STRUCTURES

Summary for 1HRJ

• Entry DOI: 10.2210/pdb1hrj/pdb
• Descriptor: HUMAN REGULATED UPON ACTIVATION NORMAL T-CELL EXPRESSED AND SECRETED (1 entity in total)
• Functional Keywords: cc chemokine, cytokine (chemotactic)
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P13501
• Total number of polymer chains: 2
• Total formula weight: 15724.02

Authors

Chung, C.,Cooke, R.M.,Proudfoot, A.E.I.,Wells, T.N.C. (deposition date: 1995-08-18, release date: 1996-10-14, Last modification date: 2024-10-16)

Primary citation

Chung, C.W.,Cooke, R.M.,Proudfoot, A.E.,Wells, T.N.
The three-dimensional solution structure of RANTES.
Biochemistry, 34:9307-9314, 1995

PubMed Abstract: The solution structure of the chemokine RANTES (regulated on activation, normal T-cell expressed and secreted) has been determined using NMR spectroscopy. Backbone and side-chain 1H and 15N assignments have been obtained using a combination of two-dimensional homonuclear and three-dimensional heteronuclear spectra. Regular elements of secondary structure have been identified on the basis of a qualitative interpretation of NOE data, J(NH-H alpha) coupling constants, and amide exchange rates. Three-dimensional structures were calculated from a total of 2146 experimental restraints using a combination of distance geometry and simulated annealing protocols. For the 13 best structures the average backbone (N, C alpha, C) atomic rmsd from the mean coordinates for residues 5-65 is 0.64 A (+/- 0.14 A) for the dimer and 0.50 A (+/- 0.08 A) for the individual monomers. Each monomer consists of a three-stranded antiparallel beta-sheet (residues 26-30, 38-43, 48-51) in a Greek key motif with a C-terminal helix (56-65) packed across the sheet, an arrangement similar to the monomeric structure of other members of this chemokine family (IL-8, PF4, MGSA/Gro alpha, and MIP-1 beta). Overall, the RANTES dimer resembles that previously reported for MIP-1 beta.

PubMed: 7542919
DOI: 10.1021/bi00029a005

Experimental method

SOLUTION NMR