rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1998-2-20
|
pubmed:databankReference |
|
pubmed:abstractText |
The structure of the two N-terminal domains of the gene 3 protein of filamentous phages (residues 1-217) has been solved by multiwavelength anomalous diffraction and refined at 1.46 A resolution. Each domain consists of either five or eight beta-strands and a single alpha-helix. Despite missing sequence homology, their cores superimposed with a root-mean-square deviation of 2 A. The domains are engaged in extensive interactions, resulting in a horseshoe shape with aliphatic amino acids and threonines lining the inside, delineating the likely binding site for the F-pilus. The glycine-rich linker connecting the domains is invisible in the otherwise highly ordered structure and may confer flexibility between the domains required during the infection process.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
1072-8368
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
5
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
140-7
|
pubmed:dateRevised |
2008-11-21
|
pubmed:meshHeading |
pubmed-meshheading:9461080-Amino Acid Sequence,
pubmed-meshheading:9461080-Capsid Proteins,
pubmed-meshheading:9461080-Crystallography, X-Ray,
pubmed-meshheading:9461080-DNA-Binding Proteins,
pubmed-meshheading:9461080-Inovirus,
pubmed-meshheading:9461080-Models, Molecular,
pubmed-meshheading:9461080-Molecular Sequence Data,
pubmed-meshheading:9461080-Peptide Library,
pubmed-meshheading:9461080-Protein Conformation,
pubmed-meshheading:9461080-Selenomethionine,
pubmed-meshheading:9461080-Sequence Homology, Amino Acid,
pubmed-meshheading:9461080-Viral Fusion Proteins
|
pubmed:year |
1998
|
pubmed:articleTitle |
The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p.
|
pubmed:affiliation |
Macromolecular Structure Laboratory, ABL-Basic Research Program, NCI-FCRDC, Frederick, Maryland 21702, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|