BMRB Entry 52175

Name: Ligand-induced transition state stabilization of protein conformational change switches the binding pathway from conformational selection to induced fit - LACTOSE
Published: 2024-02-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52175

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Ligand-induced transition state stabilization of protein conformational change switches the binding pathway from conformational selection to induced fit - LACTOSE

Deposition date:

2023-10-15

Original release date:

2024-02-22

Authors:

Stenstrom, Olof; Diehl, Carl; Modig, Kristofer; Akke, Mikael

Citation:

Citation: Stenstrom, Olof; Diehl, Carl; Modig, Kristofer; Akke, Mikael. "Ligand-induced transition state stabilization of protein conformational change switches the binding pathway from conformational selection to induced fit" Proc. Natl. Acad. Sci. U.S.A. 121, e2317747121-e2317747121 (2024).
PubMed: 38527204

Assembly members:

Assembly members:
entity_1, polymer, 138 residues, Formula weight is not available
entity_2, polymer, 2 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET9a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ALIVPYNLPLPGGVVPRMLI TILGTVKPNANRIALDFQRG NDVAFHFNPRFNENNRRVIV CNTKLDNNWGREERQSVFPF ESGKPFKIQVLVEPDHFKVA VNDAHLLQYNHRVKKLNEIS KLGISGDIDLTSASYTMI
entity_2: XX

Data sets:

heteronucl_T2_relaxation

Data type

Count

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Galectin-3C	1
2	Lactose	2

Entities:

Entity 1, Galectin-3C 138 residues - Formula weight is not available

1

ALA

LEU

ILE

VAL

PRO

TYR

ASN

LEU

PRO

LEU

2

PRO

GLY

VAL

PRO

ARG

MET

LEU

ILE

3

THR

ILE

LEU

GLY

THR

VAL

LYS

PRO

ASN

ALA

4

ASN

ARG

ILE

ALA

LEU

ASP

PHE

GLN

ARG

GLY

5

ASN

ASP

VAL

ALA

PHE

HIS

PHE

ASN

PRO

ARG

6

PHE

ASN

GLU

ASN

ARG

VAL

ILE

VAL

7

CYS

ASN

THR

LYS

LEU

ASP

ASN

TRP

GLY

8

ARG

GLU

ARG

GLN

SER

VAL

PHE

PRO

PHE

9

GLU

SER

GLY

LYS

PRO

PHE

LYS

ILE

GLN

VAL

10

LEU

VAL

GLU

PRO

ASP

HIS

PHE

LYS

VAL

ALA

11

VAL

ASN

ASP

ALA

HIS

LEU

GLN

TYR

ASN

12

HIS

ARG

VAL

LYS

LEU

ASN

GLU

ILE

SER

13

LYS

LEU

GLY

ILE

SER

GLY

ASP

ILE

ASP

LEU

14

THR

SER

ALA

SER

TYR

THR

MET

ILE

Entity 2, Lactose 2 residues - Formula weight is not available

1

GAL

BGC

Samples:

sample_1: HEPES 5 mM; Galectin-3C 0.206 mM; Lactose 0.029 mM

sample_2: HEPES 5 mM; Galectin-3C 0.205 mM; Lactose 0.058 mM

sample_3: HEPES 5 mM; Galectin-3C 0.205 mM; Lactose 0.086 mM

sample_4: HEPES 5 mM; Galectin-3C 0.204 mM; Lactose 0.166 mM

sample_5: HEPES 5 mM; Galectin-3C 0.203 mM; Lactose 0.166 mM

sample_6: HEPES 5 mM; Galectin-3C 0.302 mM; Lactose 0.248 mM

sample_7: HEPES 5 mM; Galectin-3C 0.321 mM; Lactose 0.946 mM

sample_conditions_1: ionic strength: 0.0025 M; pH: 7.4; pressure: 1 atm; temperature: 301 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N CPMG	sample_1	isotropic	sample_conditions_1
1H-15N CPMG	sample_2	isotropic	sample_conditions_1
1H-15N CPMG	sample_3	isotropic	sample_conditions_1
1H-15N CPMG	sample_4	isotropic	sample_conditions_1
1H-15N CPMG	sample_5	isotropic	sample_conditions_1
1H-15N CPMG	sample_6	isotropic	sample_conditions_1
1H-15N CPMG	sample_7	isotropic	sample_conditions_1

Software:

NMRPipe - processing

PINT - Peak Integration

NMR spectrometers:

Varian Unity 600 MHz