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Three‐dimensional structural model of the serine receptor ligand‐binding domain
Author(s) -
Jeffery Constance J.,
Koshland D.E.
Publication year - 1993
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560020407
Subject(s) - serine , homology modeling , receptor , binding site , chemistry , protein structure , ligand (biochemistry) , binding domain , biology , biochemistry , biophysics , stereochemistry , phosphorylation , enzyme
Computer‐based homology modeling techniques were used to construct a three‐dimensional model of the Escherichia coli serine receptor ligand‐binding domain based on the crystal structure of the Salmonella typhimurium aspartate receptor and the sequence homology between the two receptors. Residues that have been found in mutagenesis studies to be necessary for serine binding are located in a proposed serine‐binding site. Several other mutations that affect swimming behavior require relatively small shifts in α ‐carbon positions in the model to give a minimized structure, suggesting that small changes in receptor conformation can affect the signaling state of the receptor.