3BCH

Crystal Structure of the Human Laminin Receptor Precursor

PDB DOI: https://doi.org/10.2210/pdb3BCH/pdb

Classification: CELL ADHESION, RIBOSOMAL PROTEIN
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2007-11-12 Released: 2007-12-04
Deposition Author(s): Jamieson, K.V., Wu, J., Hubbard, S.R., Meruelo, D.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.15 Å
R-Value Free: 0.224
R-Value Work: 0.185
R-Value Observed: 0.187

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Crystal structure of the human laminin receptor precursor.

Jamieson, K.V., Wu, J., Hubbard, S.R., Meruelo, D.

(2008) J Biol Chem 283: 3002-3005

PubMed: 18063583 Search on PubMed
DOI: https://doi.org/10.1074/jbc.C700206200
Primary Citation of Related Structures:
3BCH

PubMed Abstract:
The human laminin receptor (LamR) interacts with many ligands, including laminin, prions, Sindbis virus, and the polyphenol (-)-epigallocatechin-3-gallate (EGCG), and has been implicated in a number of diseases. LamR is overexpressed on tumor cells, and targeting LamR elicits anti-cancer effects. Here, we report the crystal structure of human LamR, which provides insights into its function and should facilitate the design of novel therapeutics targeting LamR.

Organizational Affiliation

Gene Therapy Center, Cancer Institute and Department of Pathology, New York University School of Medicine, New York, New York 10016.

Macromolecule Content

Total Structure Weight: 28.21 kDa
Atom Count: 1,710
Modelled Residue Count: 197
Deposited Residue Count: 253
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
40S ribosomal protein SA	A	253	Homo sapiens	Mutation(s): 0 Gene Names: RPSA, LAMBR, LAMR1
UniProt & NIH Common Fund Data Resources
Find proteins for P08865 (Homo sapiens) Explore P08865 Go to UniProtKB: P08865
PHAROS: P08865 GTEx: ENSG00000168028
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P08865
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.15 Å
R-Value Free: 0.224
R-Value Work: 0.185
R-Value Observed: 0.187
Space Group: P 4₃ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 75.688	α = 90
b = 75.688	β = 90
c = 99.007	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2007-12-04

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2007-12-04
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2024-02-21
Changes: Data collection, Database references

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.