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Article

Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants.

The Journal of biological chemistry - 5 Sept 2003

Telmer Patrick G, Shilton Brian H

Abstract excerpt

The affinity of maltose-binding protein (MBP) for maltose and related carbohydrates was greatly increased by removal of groups in the interface opposite the ligand binding cleft. The wild-type protein has a KD of 1200 nM for maltose; mutation of residues Met-321 and Gln-325, both to alanine, resulted in a KD for maltose of 70 nM; deletion of 4 residues, Glu-172, Asn-173, Lys-175, and Tyr-176, which are part of a...

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Source

Identifiers

PMID: 12794084
DOI: 10.1074/jbc.M301004200

Genes

MBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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