Crystallization and preliminary X-ray analysis of rat SHPS-1.
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 A resolution and reduced to primitive hexagonal space group P622. Unit-cell parameters are a = b = 100.5, c = 101.3 A.
Nagata
Aki
A
Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.
Ohnishi
Hiroshi
H
Yoshimura
Masato
M
Ogawa
Akira
A
Ujita
Sayuri
S
Adachi
Hiroaki
H
Okada
Masato
M
Matozaki
Takashi
T
Nakagawa
Atsushi
A
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D017434:Protein Structure, Tertiary; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry; D051381:Rats; D011971:Receptors, Immunologic / Q000737:chemistry*
D011971:Receptors, Immunologic; C501924:Sirpa protein, rat; D017027:Protein Tyrosine Phosphatases