| dc.creator |
Piedra, David |
|
| dc.creator |
Lois, Sergi |
|
| dc.creator |
Cruz, Xavier de la |
|
| dc.date |
2008-03-20T11:34:32Z |
|
| dc.date |
2008-03-20T11:34:32Z |
|
| dc.date |
2008-01-16 |
|
| dc.date.accessioned |
2017-01-31T01:00:51Z |
|
| dc.date.available |
2017-01-31T01:00:51Z |
|
| dc.identifier |
BMC Structural Biology 2008, 8:2 |
|
| dc.identifier |
1472-6807 |
|
| dc.identifier |
http://hdl.handle.net/10261/3270 |
|
| dc.identifier |
10.1186/1472-6807-8-2 |
|
| dc.identifier.uri |
http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3270 |
|
| dc.description |
Additional material: 5 supplementary files. |
|
| dc.description |
[Background] Comparative, or homology, modelling of protein structures is the most widely used prediction method when the target protein has homologues of known structure. Given that the quality of a model may vary greatly, several studies have been devoted to identifying the factors that influence modelling results. These studies usually consider the protein as a whole, and only a few provide a separate discussion of the behaviour of biologically relevant features of the protein. Given the value of the latter for many applications, here we extended previous work by analysing the preservation of native protein clefts in homology models. We chose to examine clefts because of their role in protein function/structure, as they are usually the locus of protein-protein interactions, host the enzymes' active site, or, in the case of protein domains, can also be the locus of domain-domain interactions that lead to the structure of the whole protein. |
|
| dc.description |
[Results] We studied how the largest cleft of a protein varies in comparative models. To this end, we analysed a set of 53507 homology models that cover the whole sequence identity range, with a special emphasis on medium and low similarities. More precisely we examined how cleft quality – measured using six complementary parameters related to both global shape and local atomic environment, depends on the sequence identity between target and template proteins. In addition to this general analysis, we also explored the impact of a number of factors on cleft quality, and found that the relationship between quality and sequence identity varies depending on cleft rank amongst the set of protein clefts (when ordered according to size), and number of aligned residues. |
|
| dc.description |
[Conclusion] We have examined cleft quality in homology models at a range of seq.id. levels. Our results provide a detailed view of how quality is affected by distinct parameters and thus may help the user of comparative modelling to determine the final quality and applicability of his/her cleft models. In addition, the large variability in model quality that we observed within each sequence bin, with good models present even at low sequence identities (between 20% and 30%), indicates that properly developed identification methods could be used to recover good cleft models in this sequence range. |
|
| dc.description |
XdC acknowledges funding from the Spanish government (Grants BIO2003-09327, BIO2006-15557) and the Wellcome Trust (Research Collaboration Grant 069878/Z/02/Z). DP acknowledges economical support from the Government of Catalonia and SL from the Consejo Superior de Investigaciones Científicas. |
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| dc.description |
Peer reviewed |
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| dc.format |
18566 bytes |
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39981 bytes |
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43307 bytes |
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177842 bytes |
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881047 bytes |
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| dc.format |
22319 bytes |
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| dc.format |
application/pdf |
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| dc.format |
application/pdf |
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| dc.format |
application/pdf |
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| dc.format |
application/octet-stream |
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| dc.format |
application/pdf |
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| dc.format |
application/pdf |
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| dc.language |
eng |
|
| dc.publisher |
BioMed Central |
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| dc.relation |
Publisher’s version |
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| dc.rights |
openAccess |
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| dc.subject |
Protein structure |
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| dc.subject |
Homology models |
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| dc.subject |
Protein clefts |
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| dc.subject |
Cleft quality |
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| dc.subject |
Sequence identity |
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| dc.title |
Preservation of protein clefts in comparative models |
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| dc.type |
Artículo |
|