DP00686: Glycoprotein GFASTA viewXML view

General information
DisProt:DP00686
Name:Glycoprotein G
Synonym(s):GLYCP_NIPAV
NiV glycoprotein
NiV-G
First appeared in release:Release 5.1 (05/28/2010)
UniProt:Q9IH62
UniGene: 
SwissProt: GLYCP_NIPAV
TrEMBL:  
NCBI (GI): 82036174
Source organism:Nipah virus
Sequence length:602
Percent disordered:4%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MPAENKKVRF ENTTSDKGKI PSKVIKSYYG TMDIKKINEG LLDSKILSAF NTVIALLGSI - 60
VIIVMNIMII QNYTRSTDNQ AVIKDALQGI QQQIKGLADK IGTEIGPKVS LIDTSSTITI - 120
PANIGLLGSK ISQSTASINE NVNEKCKFTL PPLKIHECNI SCPNPLPFRE YRPQTEGVSN - 180
LVGLPNNICL QKTSNQILKP KLISYTLPVV GQSGTCITDP LLAMDEGYFA YSHLERIGSC - 240
SRGVSKQRII GVGEVLDRGD EVPSLFMTNV WTPPNPNTVY HCSAVYNNEF YYVLCAVSTV - 300
GDPILNSTYW SGSLMMTRLA VKPKSNGGGY NQHQLALRSI EKGRYDKVMP YGPSGIKQGD - 360
TLYFPAVGFL VRTEFKYNDS NCPITKCQYS KPENCRLSMG IRPNSHYILR SGLLKYNLSD - 420
GENPKVVFIE ISDQRLSIGS PSKIYDSLGQ PVFYQASFSW DTMIKFGDVL TVNPLVVNWR - 480
NNTVISRPGQ SQCPRFNTCP EICWEGVYND AFLIDRINWI SAGVFLDSNQ TAENPVFTVF - 540
KDNEILYRAQ LASEDTNAQK TITNCFLLKN KIWCISLVEI YDTGDNVIRP KLFAVKIPEQ - 600
CT



Functional narrative    

Oligomeric type II transmembrane glycoprotein that interacts with host cell surface glycoproteins ephrinB2/EFNB2 and/or ephrin B3/EFNB3 to provide virion attachment to a target cell.

Region 1: 236-245 Region 2: 579-590

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:236 - 245
Length:10
Region sequence:

RIGSCSRGVS

Modification type: Fragment
Monomeric
Native
PDB: 2VWD:A, 2VWD:B
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (277 K; gamma-butylactone (18%); Lithium chloride (0.1 M); MES (0.1 M, pH 6.0); PEG 6000 (20%))

  2. High relative B-factor

References:
  1. Bowden TA, Crispin M, Harvey DJ, Aricescu AR, Grimes JM, Jones EY, Stuart DI. "Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: a template for antiviral and vaccine design." J Virol. 2008; 82(23): 11628-36. PubMed: 18815311

Comments:
NiV-G residues 183 - 602 were used in this study.




Region 2
Type:Disordered
Name: 
Location:579 - 590
Length:12
Region sequence:

EIYDTGDNVIRP

Modification type: Fragment
Monomeric
Native
PDB: 2VWD:A, 2VWD:B
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (277 K; Gamma-butylactone (18%); Lithium chloride (0.1 M); MES (0.1 M, pH 6.0); PEG 6000 (20%))

  2. High relative B-factor

References:
  1. Bowden TA, Crispin M, Harvey DJ, Aricescu AR, Grimes JM, Jones EY, Stuart DI. "Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: a template for antiviral and vaccine design." J Virol. 2008; 82(23): 11628-36. PubMed: 18815311

Comments:
NiV-G residues 183 - 602 were used in this study.



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