PDBsum entry: 1ikm

Cytokine (chemotactic)

PDB id: 1ikm

Contents

Protein chain

69 a.a. *

* Residue conservation analysis

PDB id:

1ikm

Name:

Cytokine (chemotactic)

Title:

Nmr study of monomeric human interleukin-8 (30 structures)

Structure:

Human interleukin-8 (monomeric). Chain: a. Synonym: nap-1. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606

NMR struc:

30 models

Authors:

K.Rajarathnam,I.Clark-Lewis,B.D.Sykes

Key ref:

K.Rajarathnam et al. (1995). 1H NMR solution structure of an active monomeric interleukin-8. Biochemistry, 34, 12983-12990. PubMed id: 7548056 DOI: 10.1021/bi00040a008

Date:

03-Aug-95 Release date: 15-Oct-95

Protein chain

P10145  (IL8_HUMAN) -  Interleukin-8

Seq: 99 a.a.

Struc: 69 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (3 terms)
• Biological process: intracellular signal transduction (21 terms)
• Biochemical function: protein binding (4 terms)

DOI no: 10.1021/bi00040a008

Biochemistry 34:12983-12990 (1995)

PubMed id: 7548056

1H NMR solution structure of an active monomeric interleukin-8.

K.Rajarathnam, I.Clark-Lewis, B.D.Sykes.

ABSTRACT

The solution structure of a monomeric form of interleukin-8 (IL-8) has been solved using 1H NMR spectroscopy. The chemically synthesized nonnatural analog [IL-8 (4-72) L25 NH-->NCH3] has the same activity as that of native IL-8. Thirty structures were generated using the hybrid distance geometry and simulated annealing protocol using the program X-PLOR. The structure is well-defined except for N-terminal residues 4-6 and C-terminal residues 67-72. The rms distribution about the average structure for residues 7-66 is 0.38 A for the backbone atoms and 0.87 A for all heavy atoms. The structure consists of a series of turns and loops followed by a triple-stranded beta sheet and a C-terminal alpha helix. The structure of the monomer is largely similar to the native dimeric IL-8 structures previously determined by both NMR and X-ray methods. The major difference is that, in the monomeric analog, the C-terminal residues 67-72 are disordered whereas they are helical in the two dimeric structures. The best fit superposition of the backbone atoms of residues 7-66 of the monomer structure on the dimeric IL-8 structures showed rms differences of 1.5 and 1.2 A respectively. The turn (residues 31-35), which is disulfide linked to the N-terminal region, adopts a conformation in the monomer similar to that seen in the dimeric X-ray structure (rms difference 1.4 A) and different from that seen in the dimeric NMR structure (rms difference 2.7 A).(ABSTRACT TRUNCATED AT 250 WORDS)