Solution Structures of Human and Porcine β-Microseminoprotein

Accelerated evolution of small serum proteins (SSPs)—The PSP94 family proteins in a Japanese viper

“…3). This region may correspond to the long stretch connecting the N-and C-terminal domains as expected on the basis of the 3-D structures of human and porcine PSP94s (Ghasriani et al, 2006). It has also been identified as being the core area where extensive nonsynonymous nucleotide substitutions were found (Fig.…”

“…3. Human and porcine PSP94s are composed of two discrete domains (Ghasriani et al, 2006). The corresponding domains in SSPs were deduced on the basis of the domain structure of human PSP94, i.e., the N-terminal (residues 1-52) and C-terminal (residues 55-94) domains.…”

Crystal Structure of Prostate Secretory Protein PSP94 Shows an Edge-to-Edge Association of two Monomers to Form a Homodimer

“…The solution structure of PSP94 by NMR reported earlier by two laboratories 25,26 shows that PSP94 has two distinct domains bridged by a disulfide bond. Although the secondary structure of the individual domains reported by the two laboratories was similar, the relative orientation of the domains was very different (∼ 90°apart), giving rise to two distinct overall shapes (globular versus elongated) for this small protein.…”

Structural analysis and characterization of new small serum proteins from the serum of a venomous snake (Gloydius blomhoffii)

“…According to Ghasriani et al 14) mammalian PSP94 is a β-sheet-rich, rod-like protein with two distinct domains, N-and C-Terminal domains, as shown in Fig. 6.…”

“…14) Both have a very similar 3D structure and are β-sheet-rich proteins with two distinct domains. Although the biological function of PSP94 has not been unequivocally established, it has the ability to bind a protein in human blood (the PSP94-binding protein) and cysteine-rich secretory protein-3 (CRISP-3) from human leukocytes.…”