The crystal structures of two spermadhesins reveal the CUB domain fold

被引：129

作者：

Romero, A

Romao, MJ

Varela, PF

Kolln, I

Dias, JM

Carvalho, AL

Sanz, L

TopferPetersen, E

Calvete, JJ

机构：

[1] CSIC,CTR INVEST BIOL,E-28006 MADRID,SPAIN

[2] UNIV NOVA LISBOA,INST TECNOL QUIM & BIOL,P-2780 OEIRAS,PORTUGAL

[3] INST SUPER TECN,DEPT QUIM,P-1096 LISBON,PORTUGAL

[4] UNIV LISBON,FAC CIENCIAS,INST BIOFIS & ENGN BIOMED,LISBON,PORTUGAL

[5] TIERARZTLICHEN HSCH HANNOVER,INST REPROD MED,D-30559 HANNOVER,GERMANY

来源：

NATURE STRUCTURAL BIOLOGY | 1997年 / 4卷 / 10期

关键词：

D O I：

10.1038/nsb1097-783

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Spermadhesins, 12,000-14,000 M-r mammalian proteins, include lectins involved in sperm-egg binding and display a single CUB domain architecture. We report the crystal structures of porcine seminal plasma PSP-I/PSP-II, a heterodimer of two glycosylated spermadhesins. and bovine aSFP at 2.4 Angstrom and 1.9 Angstrom resolution respectively.

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页码：783 / 788

页数：6

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