Finding an average core structure: Application to the globins
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Citation: Russ B. Altman and Mark Gerstein. (1995) Finding an average core structure: Application to the globins. In KSL-95-17, February,1995.
| Publication techreport ( Edit ) | |
| type | Technical Report |
| bibtype | techreport |
| Bibtex basics | |
| author | Russ B. Altman and Mark Gerstein |
| title | Finding an average core structure: Application to the globins |
| number | KSL-95-17 |
| institution | Knowledge Systems, AI Laboratory |
| address | Stanford, CA, USA |
| year | 1995 |
| month | February |
| Bibtex more | |
| note | Medical Computer Science |
| Access Paper | |
| abstract | We present a procedure for automatically identifying from a set of aligned protein structures a subset of atoms with only a small amount of structural variation, i.e., a core. We apply this procedure to the globin family of proteins. Based purely on the results of the procedure, we show that the globin fold can be divided into two parts. The part with greater structural variation consists of the residues near the heme (the F helix and parts of the G and H helices), and the part with lesser structural variation (the core)forms a structural framework similar to that of the repressor protein (A, B,and E helices and remainder of the G and H helices). Such a division is consistent with many other structural and biochemical findings. In addition,we find further partitions within the core that may have biological significance. Finally, using the structural core of the globin family as a reference point, we have compared structural variation to sequence variation and shown that a core definition based on sequence conservation does not necessarily agree with one based on structural similarity. |
| KSL Technical Report ID: KSL-95-17 |
Facts about Finding an average core structure: Application to the globinsRDF feed
| Abstract | We present a procedure for automatically i … We present a procedure for automatically identifying from a set of aligned protein structures a subset of atoms with only a small amount of structural variation, i.e., a core. We apply this procedure to the globin family of proteins. Based purely on the results of the procedure, we show that the globin fold can be divided into two parts. The part with greater structural variation consists of the residues near the heme (the F helix and parts of the G and H helices), and the part with lesser structural variation (the core)forms a structural framework similar to that of the repressor protein (A, B,and E helices and remainder of the G and H helices). Such a division is consistent with many other structural and biochemical findings. In addition,we find further partitions within the core that may have biological significance. Finally, using the structural core of the globin family as a reference point, we have compared structural variation to sequence variation and shown that a core definition based on sequence conservation does not necessarily agree with one based on structural similarity. e with one based on structural similarity. |
| Address | Stanford, CA, USA + |
| Author | Russ B. Altman and Mark Gerstein + |
| Bibtype | techreport + |
| Has author | Russ B. Altman and Mark Gerstein + |
| Has identifier | KSL-95-17 + |
| Has publishing details | February,1995 + |
| Has title | Finding an average core structure: Application to the globins + |
| Has where published | KSL-95-17 + |
| Has year | 1995 + |
| Institution | Knowledge Systems, AI Laboratory + |
| Ksl tr id | KSL-95-17 + |
| Month | February + |
| Note | Medical Computer Science |
| Number | KSL-95-17 + |
| Process note | NO + |
| Title | Finding an average core structure: Application to the globins + |
| Year | 1995 + |
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