1bo9
From Proteopedia
(New page: 200px<br /> <applet load="1bo9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bo9" /> '''NMR SOLUTION STRUCTURE OF DOMAIN 1 OF HUMAN...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1bo9. | + | [[Image:1bo9.jpg|left|200px]]<br /><applet load="1bo9" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1bo9" size=" | + | |
caption="1bo9" /> | caption="1bo9" /> | ||
'''NMR SOLUTION STRUCTURE OF DOMAIN 1 OF HUMAN ANNEXIN I'''<br /> | '''NMR SOLUTION STRUCTURE OF DOMAIN 1 OF HUMAN ANNEXIN I'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1BO9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1BO9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BO9 OCA]. |
==Reference== | ==Reference== | ||
| Line 18: | Line 17: | ||
[[Category: domain 1]] | [[Category: domain 1]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:33:06 2008'' |
Revision as of 13:33, 15 February 2008
|
NMR SOLUTION STRUCTURE OF DOMAIN 1 OF HUMAN ANNEXIN I
Overview
Annexins are excellent models for studying the folding mechanisms of, multidomain proteins because they have four-eight homologous helical, domains with low identity in sequence but high similarity in folding. The, structure of an isolated domain 1 of human annexin I has been determined, by NMR spectroscopy. The sequential assignments of the 1H, 13C, and 15N, resonances of the isolated domain 1 were established by multinuclear, multidimensional NMR spectroscopy. The solution structure of the isolated, domain 1 was derived from 1,099 experimental NMR restraints using a hybrid, distance geometry-simulated annealing protocol. The root mean square, deviation of the ensemble of 20 refined conformers that represent the, structure from the mean coordinate set derived from them was 0. 57 +/-, 0.14 A and 1.11 +/- 0.19 A for the backbone atoms and all heavy atoms, respectively. The NMR structure of the isolated domain 1 could be, superimposed with a root mean square deviation of 1.36 A for all backbone, atoms with the corresponding part of the crystal structure of a truncated, human annexin I containing all four domains, indicating that the structure, of the isolated domain 1 is highly similar to that when it folded together, with the other three domains. The result suggests that in contrast to, isolated domain 2, which is largely unfolded in solution, isolated domain, 1 constitutes an autonomous folding unit and interdomain interactions may, play critical roles in the folding of annexin I.
About this Structure
1BO9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
NMR solution structure of domain 1 of human annexin I shows an autonomous folding unit., Gao J, Li Y, Yan H, J Biol Chem. 1999 Jan 29;274(5):2971-7. PMID:9915835
Page seeded by OCA on Fri Feb 15 15:33:06 2008
