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Article

Structural comparison of monomeric variants of the chemokine MIP-1beta having differing ability to bind the receptor CCR5.

Biochemistry - 11 Sept 2001

Kim S, Jao S, Laurence J S, LiWang P J

Abstract excerpt

MIP-1beta, a member of the chemokine family of proteins, tightly binds the receptor CCR5 as part of its natural function in the immune response, and in doing so also blocks the ability of many strains of HIV to enter the cell. The single most important MIP-1beta residue known to contribute to its interaction with the receptor is Phe13, which when mutated reduces the ability of MIP-1beta to bind to CCR5 by more...

Read the complete abstract on PubMed

Topics

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Share to Calorimetry
Share to Chemokine CCL4
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Macrophage Inflammatory Proteins

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Structure, Secondary

Share to Receptors, CCR5

Source

Identifiers

PMID: 11535053
DOI: 10.1021/bi011065x

Genes

MIP
CCR5

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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