6CIT: MVM NS2 NES Peptide

Crystal Structure of MVM NS2 NES Peptide in complex with CRM1-Ran-RanBP1. Determined by X-ray diffraction at 2.03 Å resolution. Released 27 Jun 2018.

Method

X-ray diffraction

Resolution

2.03 Å

Organisms

Homo sapiens, Saccharomyces cerevisiae, Minute virus of mice

Chains

4

Atoms

12,020

Mol. weight

164.16 kDa

Ligands

GNP, MG

Released

27 Jun 2018

Explore 6CIT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6CIT contains 86 α-helices and 14 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 13 helices, 7 β-strands

Molecules and chains

>6CIT_1 GTP-binding nuclear protein Ran (chains A)
METGSSHHHHHHSSGLPRGSHMAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKY
VATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYK
NVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEK
PFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL

>6CIT_2 Ran-specific GTPase-activating protein 1 (chains B)
GGSDIHFEPVVHLEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKK
TNKVRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRF
GSKENADKFKEEFEKAQEINKKA

>6CIT_3 Exportin-1 (chains C)
GGSMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQF
STNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINK
SDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQA
KALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILEL
LSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADL
KATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERE
LFKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEDLVVENDEGEIVRE
FVKESDTIQLYKSEREVLVYLTHLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGS
ISGTMSEDTEKRFVVTVIKDLLGLCEQKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLR
TVILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTA
DLQPQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSE
TVKIIANIIKTNVAVCTSMGADFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTP
KVRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNC
MTTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAF
LELPPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFI
FVSETFFVLTDSDHKSGFSKQALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQY
LANMLSNAFPHLTSEQIASFLSALTKQCKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAED
KENA

>6CIT_4 NS2 (chains D)
GGSYSTVDEMTKKFGTLTIHD

Ligands and cofactors

Water and common crystallization additives (GOL, CL) are not listed.

Primary citation

Correlation of CRM1-NES affinity with nuclear export activity. Fu, S.C., Fung, H.Y.J., Cagatay, T. et al. Mol Biol Cell (2018) 29:2037-2044. DOI 10.1091/mbc.E18-02-0096 · PubMed

Related structures

Other PDB entries of the same protein (UniProt P62826 (AlphaFold model), which also has an AlphaFold model), best resolution first:

• 3GJ0 1.48 Å, Crystal structure of human RanGDP
• 7MO5 1.55 Å, Crystal Structure of the ZnF4 of Nucleoporin NUP153 in complex with Ran-GDP
• 7MO1 1.6 Å, Crystal Structure of the ZnF1 of Nucleoporin NUP153 in complex with Ran-GDP
• 5CIQ 1.65 Å, Ran GDP wild type tetragonal crystal form
• 7MO2 1.65 Å, Crystal Structure of the ZnF2 of Nucleoporin NUP153 in complex with Ran-GDP
• 5CIT 1.75 Å, Ran GDP wild type monoclinic crystal form
• 5CIW 1.75 Å, Ran GDP Y39A mutant monoclinic crystal form
• 5CJ2 1.75 Å, Ran GDP Y39A mutant triclinic crystal form
• 1I2M 1.76 Å, Ran-RCC1-SO4 complex
• 4HAT 1.78 Å, Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1-Ran-RanBP1
• 3GJ3 1.79 Å, Crystal structure of human RanGDP-Nup153ZnF2 complex
• 3GJ5 1.79 Å, Crystal structure of human RanGDP-Nup153ZnF4 complex

Browse structure collections

About this viewer

MolViewer shows 6CIT directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.