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Crystallization and preliminary X-ray analysis of rat SHPS-1.

ABSTRACT: 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.

SUBMITTER: Nagata A

PROVIDER: S-EPMC2197194 | biostudies-literature | 2006 Mar

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of rat SHPS-1.

Nagata Aki A Ohnishi Hiroshi H Yoshimura Masato M Ogawa Akira A Ujita Sayuri S Adachi Hiroaki H Okada Masato M Matozaki Takashi T Nakagawa Atsushi A

Acta crystallographica. Section F, Structural biology and crystallization communications 20060210 Pt 3

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. Preliminar ...[more]

PMID: 16511298

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