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An improved resolution structure of the human β common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope

Date

Authors

Carr, Paul D

Conlan, F.

Ford, Sally

Ollis, David

Young, Ian

Publisher

Blackwell Publishing Ltd

Abstract

X-ray diffraction has been used to produce and refine a model of the extracellular domains of the β common cytokine receptor. A minor improvement in resolution has resulted in improved electron-density maps, which have given a clearer indication of the p

Keywords

Keywords: amino acid; CD131 antigen; cell surface receptor; CSF2RB protein, human; epitope; article; binding site; chemical structure; chemistry; human; protein conformation; X ray diffraction; Amino Acids; Binding Sites; Cytokine Receptor Common beta Subunit; Epit

URI

http://hdl.handle.net/1885/84960

Collections

Open Access Research

Source

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Type

Journal article

DOI

10.1107/S1744309106016812

Restricted until

2037-12-31

Downloads

File

Description

01_Carr_An_improved_resolution_2006.pdf (978.19 KB)