2iz3
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SOLUTION STRUCTURE OF HUMAN AND PORCINE BETA-MICROSEMINOPROTEIN
OverviewOverview
Beta-microseminoprotein (MSP) is a small cysteine-rich protein (molecular, mass about 10 kDa) first isolated from human seminal plasma and later, identified in several other organisms. The function of MSP is not known, but a recent study has shown MSP to bind CRISP-3, a protein present in, neutrophilic granulocytes. The amino acid sequence is highly variable, between species raising the question of the evolutionary conservation of, the 3D structure. Here we present NMR solution structures of both the, human and the porcine MSP. The two proteins (sequence identity 51%) have a, very similar 3D structure with the secondary structure elements well, conserved and with most of the amino acid substitutions causing a change, of charge localized to one side of the molecule. MSP is a beta-sheet-rich, protein with two distinct domains. The N-terminal domain is composed of a, four-stranded beta-sheet, with the strands arranged according to the Greek, key-motif, and a less structured part. The C-terminal domain contains two, two-stranded beta-sheets with no resemblance to known structural motifs., The two domains, connected to each other by the peptide backbone, one, disulfide bond, and interactions between the N and C termini, are oriented, to give the molecule a rather extended structure. This global fold differs, markedly from that of a previously published structure for porcine MSP, in, which the two domains have an entirely different orientation to each, other. The difference probably stems from a misinterpretation of ten, specific inter-domain NOEs.
About this StructureAbout this Structure
2IZ3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Solution structures of human and porcine beta-microseminoprotein., Ghasriani H, Teilum K, Johnsson Y, Fernlund P, Drakenberg T, J Mol Biol. 2006 Sep 22;362(3):502-15. Epub 2006 Jul 21. PMID:16930619
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