1B2T

SOLUTION STRUCTURE OF THE CX3C CHEMOKINE DOMAIN OF FRACTALKINE

1B2T の概要

• エントリーDOI: 10.2210/pdb1b2t/pdb
• NMR情報: BMRB: 4397
• 分子名称: PROTEIN (FRACTALKINE) (1 entity in total)
• 機能のキーワード: chemokine
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein. Processed fractalkine: Secreted: P78423
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8786.23

構造登録者

Handel, T.M.,Mizoue, L.S.,Bazan, J.F.,Johnson, E.C. (登録日: 1998-12-01, 公開日: 1999-04-08, 最終更新日: 2024-10-16)

主引用文献

Mizoue, L.S.,Bazan, J.F.,Johnson, E.C.,Handel, T.M.
Solution structure and dynamics of the CX3C chemokine domain of fractalkine and its interaction with an N-terminal fragment of CX3CR1.
Biochemistry, 38:1402-1414, 1999

PubMed Abstract: Fractalkine, a novel CX3C chemokine, is unusual because of both its membrane-associated structure and its direct role in cell adhesion. We have solved the solution structure of the chemokine domain of fractalkine (residues 1-76) by heteronuclear NMR methods. The 20 lowest energy structures in the ensemble have an average backbone rmsd of 0.43 A, excluding the termini. In contrast to many other chemokines which form homodimers, fractalkine's chemokine module is monomeric. Comparison of the structure to CC and CXC chemokines reveals interesting differences which are likely to be relevant to receptor binding. These include a bulge formed by the CX3C motif, the relative orientation of the N-terminus and 30's loop (residues 30-38), and the conformation of the N-loop (residues 9-19). 15N backbone relaxation experiments indicate that these same regions of the protein are dynamic. We also titrated 15N-labeled protein with a peptide from the N-terminus of the receptor CX3CR1 and confirmed that this region of the receptor contacts the fractalkine chemokine domain. Interestingly, the binding site maps roughly to the regions of greatest flexibility and structural variability. Together, these data provide a first glimpse of how fractalkine interacts with its receptor and should help guide mutagenesis studies to further elucidate the molecular details of binding and signaling through CX3CR1.

PubMed: 9931005
DOI: 10.1021/bi9820614

実験手法

SOLUTION NMR