POLIOVIRUS (TYPE 3, SABIN STRAIN) (P3/SABIN, P3/LEON/12A(1)B) COMPLEXED WITH R77975

(METHYLPYRIDAZINE PIPERIDINE ETHYLOXYPHENYL)ETHYLACETATE

Structures of poliovirus complexes with anti-viral drugs: implications for viral stability and drug design.

Binding of the Antiviral Drug Win51711 to the Sabin Strain of Type 3 Poliovirus: Structural Comparison with Drug Binding in Rhinovirus 14

Washington, Dc : American Society for Microbiology
New Aspects of Positive-Strand RNA Viruses
Role of Conformational Transitions in Poliovirus Assembly and Cell Entry

Structural Factors that Control Conformational Transitions and Serotype Specificity in Type 3 Poliovirus

Myristylation of Picornavirus Capsid Protein Vp4 and its Structural Significance

Three-Dimensional Structure of Poliovirus at 2.9 A Resolution

The Nucleotide Sequence of Poliovirus Type 3 Leon 12 A1B: Comparison with Poliovirus Type 1

THE NUMBERING OF THE VP1 RESIDUES HAS BEEN ALTERED TO FACILITATE COMPARISON WITH THE STRUCTURE OF THE MAHONEY STRAIN OF TYPE 1 POLIOVIRUS (PDB ENTRY 2PLV). MAHONEY HAS A TWO RESIDUE INSERTION, RELATIVE TO P3/SABIN, LOCATED IN THE DISORDERED N-TERMINUS OF VP1. THUS THE RESIDUES NUMBERED 24 - 302 IN THIS ENTRY ARE ACTUALLY RESIDUES 22 - 300.

GIEDLISEVAQGALTLSLPKQQDSLPDTKASGPAHSKEVPALTAVETGATNPLAPSDTVQTRHVVQRRSRSESTIESFFA
RGACVAIIEVDNEQPTTRAQKLFAMWRITYKDTVQLRRKLEFFTYSRFDMEFTFVVTANFTNANNGHALNQVYQIMYIPP
GAPTPKSWDDYTWQTSSNPSIFYTYGAAPARISVPYVGLANAYSHFYDGFAKVPLKTDANDQIGDSLYSAMTVDDFGVLA
VRVVNDHNPTKVTSKVRIYMKPKHVRVWCPRPPRAVPYYGPGVDYRNNLDPLSEKGLTTY

SPNVEACGYSDRVLQLTLGNSTITTQEAANSVVAYGRWPEFIRDDEANPVDQPTEPDVATCRFYTLDTVMWGKESKGWWW
KLPDALRDMGLFGQNMYYHYLGRSGYTVHVQCNASKFHQGALGVFAIPEYCLAGDSDKQRYTSYANANPGERGGKFYSQF
NKDNAVTSPKREFCPVDYLLGCGVLLGNAFVYPHQIINLRTNNSATIVLPYVNALAIDSMVKHNNWGIAILPLSPLDFAQ
DSSVEIPITVTIAPMCSEFNGLRNVTAPKFQ

GLPVLNTPGSNQYLTSDNHQSPCAIPEFDVTPPIDIPGEVKNMMELAEIDTMIPLNLESTKRNTMDMYRVTLSDSADLSQ
PILCLSLSPAFDPRLSHTMLGEVLNYYTHWAGSLKFTFLFCGSMMATGKILVAYAPPGAQPPTSRKEAMLGTHVIWDLGL
QSSCTMVVPWISNVTYRQTTQDSFTEGGYISMFYQTRIVVPLSTPKSMSMLGFVSACNDFSVRLLRDTTHISQSA

P3/SABIN PREPARED FROM A LOW-PASSAGE SEED STOCK OF A PLAQUE ISOLATE (P3/LEON/12A(1)B PLACQUE 411) OBTAINED FROM P.D.MINOR (NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS CONTROL, LONDON)
Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)

THE APPROPRIATE SEQUENCE FOR THIS VIRUS CORRESPONDS TO THE STANWAY ET AL. REFERENCE ABOVE.

THE NUMBERING OF THE VP1 RESIDUES HAS BEEN ALTERED TO FACILITATE COMPARISON WITH THE STRUCTURE OF THE MAHONEY STRAIN OF TYPE 1 POLIOVIRUS (PDB ENTRY 2PLV). MAHONEY HAS A TWO RESIDUE INSERTION, RELATIVE TO P3/SABIN, LOCATED IN THE DISORDERED N-TERMINUS OF VP1. THUS THE RESIDUES NUMBERED 24 - 302 IN THIS ENTRY ARE ACTUALLY RESIDUES 22 - 300.

VP4 HAS A MYRISTATE MOIETY COVALENTLY LINKED TO ITS N-TERMINUS. THIS MYRISTATE HAS BEEN DESIGNATED RESIDUE 1 OF VP4 AND THE AMINO ACID RESIDUES OF VP4 ARE NUMBERED 2 - 69.

icosahedral asymmetric unit, std point frame

STEREOCHEMICAL CONSTRAINTS BASED ON PARAM19 AND TOP19
FILES USED IN X-PLOR VERSIONS PREVIOUS TO VERSION 3.1
ATOMIC MODELS FOR THE VIRUS AND THE DRUG WERE BUILT TO FIT
ICOSAHEDRALLY CONSTRAINED 'FO' MAP USING THE GRAPHICS
PROGRAM FRODO (JONES, 1978) MODIFIED TO INCORPORATE T = 1
ICOSAHEDRAL SYMMETRY. ATOMIC MODELS WERE OPTIMIZED WITH
RESPECT TO THIS MAP BY A PSEUDO-REAL-SPACE REFINEMENT
PROCEDURE, MINIMIZING A RESIDUAL WITH A STEREOCHEMICAL AND
A CRYSTALLOGRAPHIC COMPONENT. THE GRADIENT OF THE
STEREOCHEMICAL COMPONENT WAS PROVIDED BY THE X-PLOR
PROGRAM (A. BRUNGER, X-PLOR VERSION 2.1 YALE UNIVERSITY
1990). THE CRYSTALLOGRAPHIC COMPONENT AND ITS GRADIENT
WERE EVALUATED OVER THE VOLUME OF AN ARBITRARY PSEUDO-CELL
(THE PROTOMER BOX) WHICH IS SUFFICIENTLY LARGE TO
COMFORTABLY ENCLOSE A COMPLETE CHEMICALLY CONTINUOUS
POLIOVIRUS PROTOMER, TOGETHER WITH WHATEVER FRAGMENTS OF
SYMMETRY-RELATED PROTOMERS HAPPEN TO LIE SUFFICIENTLY
CLOSE TO THE BOX TO CONTRIBUTE TO IT. THIS REFINEMENT
SEEKS TO MINIMIZE THE DISCREPANCY BETWEEN THE 'PHASED'
FOURIER TRANSFORMS OF MODEL-BASED ELECTRON DENSITY AND
AUTHENTIC SYMMETRY-CONSTRAINED ELECTRON DENSITY, WHEN EACH
TRANSFORM IS CALCULATED IN THE ARBITRARY PROTOMER BOX
VOLUME, SCALED IN A RESOLUTION-DEPENDENT FASHION.
SEE JRNL REFERENCE FOR MORE DETAILS.
THE DISORDERED RESIDUES ABSENT FROM THE MODEL INCLUDE
THE AMINO TERMINUS OF VP1 PRIOR TO THE RESIDUE LABELED
GLN 24, 1 - 5 IN VP2, 236 - 238 IN VP3, AND THE RESIDUES
LABELED 17 - 22 IN VP4.
THE POLYPEPTIDE DESIGNATED IN THIS FILE AS RESIDUES 6 - 9
OF CHAIN 0 REPRESENTS A FEATURE IN THE ELECTRON DENSITY MAP
WHICH APPEARS TO BE A BETA STRAND. ALTHOUGH THE SIDE
CHAINS OF THIS STRAND CANNOT BE CORRELATED RELIABLY WITH
THE SEQUENCE OF THE PROTEIN, THE FEATURE IS BELIEVED LIKELY
TO CORRESPOND TO SOME PORTION OF THE AMINO TERMINAL
EXTENSION OF VP1. NO SOLVENT MOLECULES ARE INCLUDED.

THE POLYPEPTIDE DESIGNATED IN THIS FILE AS RESIDUES 6 - 9
OF CHAIN 0 REPRESENTS A FEATURE IN THE ELECTRON DENSITY MAP
WHICH APPEARS TO BE A BETA STRAND. ALTHOUGH THE SIDE
CHAINS OF THIS STRAND CANNOT BE CORRELATED RELIABLY WITH
THE SEQUENCE OF THE PROTEIN, THE FEATURE IS BELIEVED LIKELY
TO CORRESPOND TO SOME PORTION OF THE AMINO TERMINAL
EXTENSION OF VP1.

POLIOVIRUS TYPE 3, (METHYLPYRIDAZINE PIPERIDINE ETHYLOXYPHENYL)ETHYLACETATE

VIRUS COAT PROTEIN, HYDROLASE, THIOL PROTEASE, Icosahedral virus, Virus