1vqd: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vqd OCA], [http://www.ebi.ac.uk/pdbsum/1vqd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vqd RCSB]</span>
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==About this Structure==
==About this Structure==
1VQD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_f1 Bacteriophage f1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQD OCA].  
1VQD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_f1 Enterobacteria phage f1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQD OCA].  


==Reference==
==Reference==
Potential use of additivity of mutational effects in simplifying protein engineering., Skinner MM, Terwilliger TC, Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10753-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8855252 8855252]
Potential use of additivity of mutational effects in simplifying protein engineering., Skinner MM, Terwilliger TC, Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10753-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8855252 8855252]
[[Category: Bacteriophage f1]]
[[Category: Enterobacteria phage f1]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Skinner, M M.]]
[[Category: Skinner, M M.]]
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[[Category: mutant]]
[[Category: mutant]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:27:16 2008''

Revision as of 00:27, 31 March 2008

File:1vqd.jpg


PDB ID 1vqd

Drag the structure with the mouse to rotate
, resolution 1.82Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY LEU 47 (V35I, I47L)


OverviewOverview

The problem of rationally engineering protein molecules can be simplified where effects of mutations on protein function are additive. Crystal structures of single and double mutants in the hydrophobic core of gene V protein indicate that structural and functional effects of core mutations are additive when the regions structurally influenced by the mutations do not substantially overlap. These regions of influence can provide a simple basis for identifying sets of mutations that will show additive effects.

About this StructureAbout this Structure

1VQD is a Single protein structure of sequence from Enterobacteria phage f1. Full crystallographic information is available from OCA.

ReferenceReference

Potential use of additivity of mutational effects in simplifying protein engineering., Skinner MM, Terwilliger TC, Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10753-7. PMID:8855252

Page seeded by OCA on Mon Mar 31 00:27:16 2008

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