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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1995-7-13
|
| pubmed:abstractText |
Proteins can interact with short peptide sequences in a variety of ways that can be sequence dependent or independent. The bound peptides are frequently in an extended conformation but may also adopt beta-turns or alpha-helices as motifs for recognition. The peptides can be completely buried in cavities, bound in grooves or pockets, or form beta-strand type interactions at the protein surface. These various recognition motifs are illustrated by peptide interactions with antibodies, calmodulin, OppA periplasmic binding protein, PapD chaperone, MHC class I and class II molecules, and Src homology (SH) domains 2 and 3.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0959-440X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
5
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
103-13
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:7773739-Amino Acid Sequence,
pubmed-meshheading:7773739-Binding Sites,
pubmed-meshheading:7773739-Molecular Sequence Data,
pubmed-meshheading:7773739-Peptides,
pubmed-meshheading:7773739-Protein Binding,
pubmed-meshheading:7773739-Protein Conformation,
pubmed-meshheading:7773739-Proteins
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Protein-peptide interactions.
|
| pubmed:affiliation |
Department of Molecular Biology MB13, Scripps Research Institute, La Jolla, CA 92037, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
|