Crystal Structure of the Cysteine-rich Secretory Protein Stecrisp Reveals That the Cysteine-rich Domain Has a K+ Channel Inhibitor-like Fold

Guo, Min; Teng, Maikun; Niu, Liwen; Liu, Qun; Huang, Qingqiu; Hao, Quan

doi:10.1074/jbc.m413566200

Cited by 138 publications

(135 citation statements)

References 55 publications

(55 reference statements)

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Section: Introductionsupporting

confidence: 76%

“…The C-terminal domain of CRISP-3 has structural similarity to potassium-channel inhibitors [5] and several reptile CRISPs can inhibit different ion-channels [4]. Recently, CRISP-1 in rats was shown to inhibit capacitation of spermatozoa and thus prevent premature sperm activation [17].…”

Section: Discussionmentioning

confidence: 99%

“…It belongs to a family of CRISPs found in mammals and reptiles, which is characterized by 16 highly conserved cysteine residues of a total of 220-230 amino acids and 35-85% identity in the primary structure [2][3][4]. Recently, the crystal structure of a snake venom CRISP was elucidated [5]. This confirmed the previously proposed two-domain structure of CRISPs with a large N-terminal SCP domain (after sperm coating protein, an alternative name for murine CRISP-1) and a smaller, compact C-terminal domain, separated by a hinge-region [3,5].…”

Section: Introductionmentioning

confidence: 99%

“…Recently, the crystal structure of a snake venom CRISP was elucidated [5]. This confirmed the previously proposed two-domain structure of CRISPs with a large N-terminal SCP domain (after sperm coating protein, an alternative name for murine CRISP-1) and a smaller, compact C-terminal domain, separated by a hinge-region [3,5].A novel protein with an N-terminal SCP domain has been identified in human blood plasma and is called PSP94-binding protein (PSPBP) as it binds to β -microseminoprotein (MSP), also known as prostate secretory protein of 94 amino acids (PSP94) [6]. MSP is one of the three predominant proteins secreted by the prostate gland, but it is also present in other body fluids, e.g., tracheobronchial fluid.…”

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confidence: 99%

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β-Microseminoprotein binds CRISP-3 in human seminal plasma

Udby

Lundwall

Johnsen

et al. 2005

Biochemical and Biophysical Research Communications

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Abstractβ -Microseminoprotein (MSP) and cysteine-rich secretory protein 3 (CRISP-3) are abundant constituents of human seminal plasma. Immunoprecipitation and gel filtration of seminal plasma proteins combined with examination of the proteins in their pure form showed that MSP and CRISP-3 form stable, non-covalent complexes. CRISP-3 binds MSP with very high affinity, as evidenced by surface plasmon resonance. Due to far higher abundance of MSP in prostatic fluid, it manifests large overcapacity for CRISP-3 binding. Structural similarity with an MSP-binding protein from blood plasma suggests that CRISP-3 binds MSP through its aminoterminal SCP-domain. KeywordsCysteine-rich secretory protein; β-Microseminoprotein; PSP94; Seminal plasma; Prostate cancer; Protein complex; SCP-domain; Mass spectrometry; Surface plasmon resonance Human cysteine-rich secretory protein 3 (CRISP-3; also known as SGP28) was first isolated from neutrophilic granulocytes, but it is also a constituent of blood plasma and exocrine secretions, such as saliva and seminal plasma [1]. It belongs to a family of CRISPs found in mammals and reptiles, which is characterized by 16 highly conserved cysteine residues of a total of 220-230 amino acids and 35-85% identity in the primary structure [2][3][4]. Recently, the crystal structure of a snake venom CRISP was elucidated [5]. This confirmed the previously proposed two-domain structure of CRISPs with a large N-terminal SCP domain (after sperm coating protein, an alternative name for murine CRISP-1) and a smaller, compact C-terminal domain, separated by a hinge-region [3,5].A novel protein with an N-terminal SCP domain has been identified in human blood plasma and is called PSP94-binding protein (PSPBP) as it binds to β -microseminoprotein (MSP), also known as prostate secretory protein of 94 amino acids (PSP94) [6]. MSP is one of the three predominant proteins secreted by the prostate gland, but it is also present in other body fluids, e.g., tracheobronchial fluid. In general, MSP-synthesis is associated with tissue producing [7,8].It is yet unknown whether MSP binds to PSPBP through the SCP domain or via the large C-terminal part of the molecule [6]. One way to answer this question is to investigate whether MSP binds other proteins with an SCP domain, and the abundance of both MSP and CRISP-3 in human seminal plasma prompted us to test the hypothesis that these proteins form high-affinity complexes. Materials and methods MaterialsHuman MSP was purified from seminal plasma with the method described for the purification of pig MSP [9]. Human CRISP-3 was purified from granulocytes [10]. Specific antisera were raised in rabbits against recombinant C-terminally truncated human CRISP-3 and native human MSP [1,11]. Semen was collected from healthy volunteers and allowed to liquefy for 1 h at room temperature (RT), followed by centrifugation to remove spermatozoa and was subsequently stored at −20 °C until use. Gel filtrationProteins were separated according to their molecular size by gel filtration on a Su...

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Section: Introductionsupporting

confidence: 76%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

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β-Microseminoprotein binds CRISP-3 in human seminal plasma

Udby

Lundwall

Johnsen

et al. 2005

Biochemical and Biophysical Research Communications

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“…The coordinating residues for cadmium or zinc binding have been clearly predicted from the X-ray crystallographic structures of Crisp snake toxins (Wang et al 2005 ; Guo et al 2005 ;Shikamoto et al 2005 ). Similarly, the structure of the Crisp-related protein glioma pathogenesis-related protein 1 in its zinc bound form has been determined (Asojo et al 2011 ).…”

Section: The Future Of Crisp Protein Relationships In Reproductionmentioning

confidence: 99%

Allurin: Exploring the Activity of a Frog Sperm Chemoattractant in Mammals

Burnett

Sugiyama

Washburn

et al. 2014

Sexual Reproduction in Animals and Plants

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Allurin, a 21-kDa protein secreted by the oviduct of female Xenopus frogs, is incorporated into the jelly layers of eggs as they pass single fi le on their way to the uterus and subsequent spawning. Hydration of the egg jelly layers at spawning releases allurin as a chemoattractant that binds to the midpiece of Xenopus sperm in a dose-dependent manner. Gradients of allurin elicit directed swimming across a porous membrane in two-chamber assays and preferential, up-gradient swimming of sperm in video-microscopic assays. Allurin, purifi ed from X. laevis or produced in recombinant form, also elicits chemotaxis by mouse sperm in twochamber and video microscopic assays. Allurin binds to mouse sperm at the midpiece and head, a pattern also seen in frog sperm. Western blots suggest the presence of an allurin-like protein in the follicular fl uid of mice and humans and peptides that mimic subdomains within allurin elicit chemoattractive behavior in both mouse and human sperm. By sequence homology, allurin is a truncated member of the CysteineRIch Secretory Protein (CRISP) family whose members include Crisps 1, 2, and 4, which have been demonstrated to modulate mammalian sperm functions including Dedication This chapter is dedicated to Allan L. Bieber, a long-time collaborator of ours who recently passed on. Allan was an expert biochemist who guided our purifi cation of allurin and characterization of its disulfi de bonding pattern using mass spectrometry. His long-term interest in venom proteins from snakes was culminated by his delight in fi nding that allurin is closely related to Crisp snake toxin proteins.

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The function of yeast CAP family proteins in lipid export, mating, and pathogen defense

et al. 2017

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In their natural habitat, yeast cells are constantly challenged by changing environmental conditions and a fierce competition for limiting resources. To thrive under such conditions, cells need to adapt and divide quickly, and be able to neutralize the toxic compounds secreted by their neighbors. Proteins like the pathogen‐related yeast, Pry proteins, which belong to the large CAP/SCP/TAPS superfamily, may have an important role in this function. CAP proteins are conserved from yeast to man and are characterized by a unique αβα sandwich fold. They are mostly secreted glycoproteins and have been implicated in many different physiological processes including pathogen defense, virulence, venom toxicity, and sperm maturation. Yeast members of this family bind and export sterols as well as fatty acids, and they render cells resistant to eugenol, an antimicrobial compound present in clove oil. CAP family members might thus exert their various physiological functions through binding, sequestration, and neutralization of such small hydrophobic compounds.

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Crystal Structure of the Cysteine-rich Secretory Protein Stecrisp Reveals That the Cysteine-rich Domain Has a K+ Channel Inhibitor-like Fold

Abstract: Stecrisp from

Cited by 138 publications

References 55 publications

β-Microseminoprotein binds CRISP-3 in human seminal plasma

β-Microseminoprotein binds CRISP-3 in human seminal plasma

Allurin: Exploring the Activity of a Frog Sperm Chemoattractant in Mammals

The function of yeast CAP family proteins in lipid export, mating, and pathogen defense

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