Structural highlights
3mcb is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | |
| Related: | 3mce |
| Gene: | Alpha NAC, HSD48, NACA (HUMAN), Beta NAC (BTF3b), BTF3, NACB, OK/SW-cl.8 (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[NACA_HUMAN] Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters.[1] [2] [3] [BTF3_HUMAN] General transcription factor. BTF3 can form a stable complex with RNA polymerase II. Required for the initiation of transcription.
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 PubMed
Nascent polypeptide associated complex (NAC) and its two isolated subunits, alphaNAC and betaNAC, play important roles in nascent peptide targeting. We determined a 1.9 A resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 A resolution crystal structure of alphaNAC NAC domain homodimer. These structures provide detailed information of NAC heterodimerization and alphaNAC homodimerization. We found that the NAC domains of alphaNAC and betaNAC share very similar folding despite of their relative low identity of amino acid sequences. Furthermore, different electric charge distributions of the two subunits at the NAC interface provide an explanation to the observation that the heterodimer of NAC complex is more stable than the single subunit homodimer. In addition, we successfully built a betaNAC NAC domain homodimer model based on homologous modeling, suggesting that NAC domain dimerization is a general property of the NAC family. These 3D structures allow further studies on structure-function relationship of NAC.
Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its alphaNAC subunit.,Wang L, Zhang W, Wang L, Zhang XC, Li X, Rao Z Protein Cell. 2010 Apr;1(4):406-16. Epub 2010 May 8. PMID:21203952[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Moller I, Beatrix B, Kreibich G, Sakai H, Lauring B, Wiedmann M. Unregulated exposure of the ribosomal M-site caused by NAC depletion results in delivery of non-secretory polypeptides to the Sec61 complex. FEBS Lett. 1998 Dec 11;441(1):1-5. PMID:9877153
- ↑ Beatrix B, Sakai H, Wiedmann M. The alpha and beta subunit of the nascent polypeptide-associated complex have distinct functions. J Biol Chem. 2000 Dec 1;275(48):37838-45. PMID:10982809 doi:10.1074/jbc.M006368200
- ↑ Lopez S, Stuhl L, Fichelson S, Dubart-Kupperschmitt A, St Arnaud R, Galindo JR, Murati A, Berda N, Dubreuil P, Gomez S. NACA is a positive regulator of human erythroid-cell differentiation. J Cell Sci. 2005 Apr 15;118(Pt 8):1595-605. Epub 2005 Mar 22. PMID:15784678 doi:jcs.02295
- ↑ Wang L, Zhang W, Wang L, Zhang XC, Li X, Rao Z. Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its alphaNAC subunit. Protein Cell. 2010 Apr;1(4):406-16. Epub 2010 May 8. PMID:21203952 doi:10.1007/s13238-010-0049-3
