Computational studies of CXCR1, the receptor of IL-8/CXCL8, using molecular dynamics and electrostatics.

Computational studies of CXCR1, the receptor of IL-8/CXCL8, using molecular dynamics and electrostatics. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Computational studies of CXCR1, the receptor of IL-8/CXCL8, using molecular dynamics and electrostatics. Abstract Text:

Nicholas Huynh,Buddhadeb Mallik,Li Zhang,Manuela Martins-Green,Dimitrios Morikis,Nicholas Huynh,Buddhadeb Mallik,Li Zhang,Manuela Martins-Green,Dimitrios Morikis,Nicholas Huynh,Buddhadeb Mallik,Li Zhang,Manuela Martins-Green,Dimitrios Morikis,

The three-dimensional structure of IL-8/CXCL8 has been previously determined using NMR spectroscopy and X-ray crystallography, but the structure of the receptors for this chemokine has not been determined experimentally. We present here the development of a model for the structure of the IL-8/CXCL8 receptor CXCR1, using a combination of homology modeling and a molecular dynamics simulation. Based on this model, we discuss the analysis of structural, dynamic, and physicochemical properties of CXCR1. We focused on the role of pairwise ionic interactions in local structural stability of CXCR1 and the role of electrostatic potentials in recognition of CXCR1 with IL-8/CXCL8. We have performed theoretical mutations of six charged amino acids in CXCR1, which abolish binding as suggested by earlier experimental data, to shed light on the effect of charge on association ability. We propose that the observed loss of binding in the six CXCR1 mutants is owed to loss of local structural stability, rather than hindrance of the recognition process because of changes in the overall electrostatic properties of the receptor. Based on further structural analysis, we propose some mutations of charged residues involving ion pairs in different elements of transmembrane helices and extracellular loops, which are expected to alter the local structure and possibly affect binding.

Computational studies of CXCR1, the receptor of IL-8/CXCL8, using molecular dynamics and electrostatics. Publishing Authors By Initials

N Huynh,B Mallik,L Zhang,M Martins-Green,D Morikis,N Huynh,B Mallik,L Zhang,M Martins-Green,D Morikis,N Huynh,B Mallik,L Zhang,M Martins-Green,D Morikis,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Computational studies of CXCR1, the receptor of IL-8/CXCL8, using molecular dynamics and electrostatics. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Biopolymers

VOLUME: 89

Page Numbers: 52-61

Journal Abbreviation: Biopolymers

ISSN: 0006-3525

DAY: 6

MONTH: Jan

YEAR: 2008

Computational studies of CXCR1, the receptor of IL-8/CXCL8, using molecular dynamics and electrostatics. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 372525

Computational studies of CXCR1, the receptor of IL-8/CXCL8, using molecular dynamics and electrostatics. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Computational studies of CXCR1, the receptor of IL-8/CXCL8, using molecular dynamics and electrostatics. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Computational studies of CXCR1, the receptor of IL-8/CXCL8, using molecular dynamics and electrostatics.

AFFILIATION: Department of Biochemistry, University of California, Riverside, CA 92521, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM-069736

ACRONYM: GM

MEDLINETA: Biopolymers

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Computational studies of CXCR1, the receptor of IL-8/CXCL8, using molecular dynamics and electrostatics Related Publications

• Computational studies of CXCR1, the receptor of IL-8/CXCL8, using molecular dynamics and electrostatics.
• Immunophysical exploration of C3d-CR2(CCP1-2) interaction using molecular dynamics and electrostatics.
• Solution structure of a bent alpha-helix.
• Toward full-sequence de novo protein design with flexible templates for human Beta-defensin-2.
• pH Dependence of Stability of the 10th Human Fibronectin Type III Domain: A Computational Study.