Crystal structure of the human laminin receptor precursor

Kelly V. Jamieson; Jinhua Wu; Stevan R. Hubbard; Daniel Meruelo

doi:10.1074/jbc.C700206200

Crystal structure of the human laminin receptor precursor

Kelly V. Jamieson, Jinhua Wu, Stevan R. Hubbard, Daniel Meruelo

Cancer Signaling and Microenvironment (CSM)

New York University

Research output: Contribution to journal › Article › peer-review

48 Scopus citations

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.

Original language	English
Pages (from-to)	3002-3005
Number of pages	4
Journal	Journal of Biological Chemistry
Volume	283
Issue number	6
DOIs	https://doi.org/10.1074/jbc.C700206200
State	Published - Feb 8 2008

Keywords

Amino Acid Sequence
Animals
Caenorhabditis elegans
Crystallography, X-Ray
Humans
Ligands
Models, Molecular
Molecular Conformation
Molecular Sequence Data
Protein Binding
Protein Precursors/chemistry
Receptors, Cell Surface/chemistry
Receptors, Laminin/chemistry
Saccharomyces cerevisiae
Sequence Homology, Amino Acid

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1074/jbc.C700206200

Cite this

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title = "Crystal structure of the human laminin receptor precursor",

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.",

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author = "Jamieson, {Kelly V.} and Jinhua Wu and Hubbard, {Stevan R.} and Daniel Meruelo",

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doi = "10.1074/jbc.C700206200",

language = "English",

volume = "283",

pages = "3002--3005",

journal = "Journal of Biological Chemistry",

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T1 - Crystal structure of the human laminin receptor precursor

AU - Jamieson, Kelly V.

AU - Wu, Jinhua

AU - Hubbard, Stevan R.

AU - Meruelo, Daniel

PY - 2008/2/8

Y1 - 2008/2/8

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Animals

KW - Caenorhabditis elegans

KW - Crystallography, X-Ray

KW - Humans

KW - Ligands

KW - Models, Molecular

KW - Molecular Conformation

KW - Molecular Sequence Data

KW - Protein Binding

KW - Protein Precursors/chemistry

KW - Receptors, Cell Surface/chemistry

KW - Receptors, Laminin/chemistry

KW - Saccharomyces cerevisiae

KW - Sequence Homology, Amino Acid

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U2 - 10.1074/jbc.C700206200

DO - 10.1074/jbc.C700206200

M3 - Article

C2 - 18063583

AN - SCOPUS:41249088465

SN - 0021-9258

VL - 283

SP - 3002

EP - 3005

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 6

ER -

Crystal structure of the human laminin receptor precursor

Abstract

Keywords

UN SDGs

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