Open AccessCrystallization and preliminary X‐ray analysis of rat SHPS‐1
Author(s) -
Nagata Aki,
Ohnishi Hiroshi,
Yoshimura Masato,
Ogawa Akira,
Ujita Sayuri,
Adachi Hiroaki,
Okada Masato,
Matozaki Takashi,
Nakagawa Atsushi
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106001941
Subject(s) - transmembrane protein , crystallography , ligand (biochemistry) , biophysics , crystallization , receptor , cd47 , chemistry , microbiology and biotechnology , biology , biochemistry , organic chemistry
SHPS‐1, a receptor‐type transmembrane protein, is abundantly expressed in neural and myeloid tissues. The most amino‐terminal immunoglobulin‐like domain of SHPS‐1 plays an important role in a variety of cell functions by binding its ligand CD47. Interaction between SHPS‐1 and CD47 is thought to be involved in negative regulation of phagocytosis. The ligand‐binding domain of rat SHPS‐1 was purified and crystallized using the vapour‐diffusion method with the solution‐stirring technique. Preliminary X‐ray diffraction data were collected from SHPS‐1 crystals to 2.8 Å resolution and reduced to primitive hexagonal space group P 622. Unit‐cell parameters are a = b = 100.5, c = 101.3 Å.