3n89
From Proteopedia
KH domains
Structural highlights
Function[GLD3_CAEEL] Required maternally for germline survival and embryogenesis. Forms a complex with gls-1 which promotes the oogenic cell fate by freeing the translational repressor fbf to repress sperm promoting factors. Promotes maturation of primary spermatocytes to mature sperm. Required during hermaphrodite development to promote sperm fate, which is critical for determining the normal number of sperm. Promotion of sperm fate is at the expense of oogenesis, possibly through the negative regulation of fbf. Required during male development for the continued production of sperm and inhibition of oogenesis. Together with gld-2, promotes the transition from mitosis to meiosis.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCaenorhabditis elegans GLD-3 is a five K homology (KH) domain-containing protein involved in the translational control of germline-specific mRNAs during embryogenesis. GLD-3 interacts with the cytoplasmic poly(A)-polymerase GLD-2. The two proteins cooperate to recognize target mRNAs and convert them into a polyadenylated, translationally active state. We report the 2.8-A-resolution crystal structure of a proteolytically stable fragment encompassing the KH2, KH3, KH4, and KH5 domains of C. elegans GLD-3. The structure reveals that the four tandem KH domains are organized into a globular structural unit. The domains are involved in extensive side-by-side interactions, similar to those observed in previous structures of dimeric KH domains, as well as head-to-toe interactions. Small-angle X-ray scattering reconstructions show that the N-terminal KH domain (KH1) forms a thumb-like protrusion on the KH2-KH5 unit. Although KH domains are putative RNA-binding modules, the KH region of GLD-3 is unable in isolation to cross-link RNA. Instead, the KH1 domain mediates the direct interaction with the poly(A)-polymerase GLD-2, pointing to a function of the KH region as a protein-protein interaction platform. Four KH domains of the C. elegans Bicaudal-C ortholog GLD-3 form a globular structural platform.,Nakel K, Hartung SA, Bonneau F, Eckmann CR, Conti E RNA. 2010 Sep 7. PMID:20823118[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Caeel | Bonneau, F | Conti, E | Eckmann, C R | Hartung, S A | Nakel, K | Cell cycle | Germline development | Kh domain | Rna binding
