2aqz
From Proteopedia
(New page: 200px<br /> <applet load="2aqz" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aqz, resolution 1.85Å" /> '''Crystal structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2aqz.gif|left|200px]]<br /> | + | [[Image:2aqz.gif|left|200px]]<br /><applet load="2aqz" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2aqz" size=" | + | |
caption="2aqz, resolution 1.85Å" /> | caption="2aqz, resolution 1.85Å" /> | ||
'''Crystal structure of FGF-1, S17T/N18T/G19 deletion mutant'''<br /> | '''Crystal structure of FGF-1, S17T/N18T/G19 deletion mutant'''<br /> | ||
| Line 6: | Line 5: | ||
==Overview== | ==Overview== | ||
Human acidic fibroblast growth factor (FGF-1) is a member of the, beta-trefoil superfold, a protein architecture that exhibits a, characteristic threefold axis of structural symmetry. FGF-1 contains 11, beta-turns, the majority being type I 3:5; however, a type I 4:6 turn is, also found at three symmetry-related locations. The relative uniqueness of, the type I 4:6 turn in the FGF-1 structure suggests it may play a key role, in the stability, folding, or function of the protein. To test this, hypothesis a series of deletion mutations were constructed, the aim of, which was to convert existing type I 4:6 turns at two locations into type, I 3:5 turns. The results show it is possible to successfully substitute, the type I 4:6 turn by a type I 3:5 turn with minimal impact upon protein, stability or folding. Thus, these different turn structures, even though, they differ in length, exhibit similar energetic properties. Additional, sequence swapping mutations within the introduced type I 3:5 turns, suggests that the turn sequence primarily affects stability but not turn, structure (which appears dictated primarily by the local environment)., Although the results suggest that a stable, foldable beta-trefoil protein, may be designed utilizing a single turn type (type I 3:5), a type I 4:6, turn at turn 1 of FGF-1 appears essential for efficient mitogenic, function. | Human acidic fibroblast growth factor (FGF-1) is a member of the, beta-trefoil superfold, a protein architecture that exhibits a, characteristic threefold axis of structural symmetry. FGF-1 contains 11, beta-turns, the majority being type I 3:5; however, a type I 4:6 turn is, also found at three symmetry-related locations. The relative uniqueness of, the type I 4:6 turn in the FGF-1 structure suggests it may play a key role, in the stability, folding, or function of the protein. To test this, hypothesis a series of deletion mutations were constructed, the aim of, which was to convert existing type I 4:6 turns at two locations into type, I 3:5 turns. The results show it is possible to successfully substitute, the type I 4:6 turn by a type I 3:5 turn with minimal impact upon protein, stability or folding. Thus, these different turn structures, even though, they differ in length, exhibit similar energetic properties. Additional, sequence swapping mutations within the introduced type I 3:5 turns, suggests that the turn sequence primarily affects stability but not turn, structure (which appears dictated primarily by the local environment)., Although the results suggest that a stable, foldable beta-trefoil protein, may be designed utilizing a single turn type (type I 3:5), a type I 4:6, turn at turn 1 of FGF-1 appears essential for efficient mitogenic, function. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602115 602115]], LADD syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602115 602115]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2AQZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2AQZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AQZ OCA]. |
==Reference== | ==Reference== | ||
| Line 22: | Line 18: | ||
[[Category: beta-trefoil]] | [[Category: beta-trefoil]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:23:25 2008'' |
Revision as of 13:23, 23 January 2008
|
Crystal structure of FGF-1, S17T/N18T/G19 deletion mutant
Overview
Human acidic fibroblast growth factor (FGF-1) is a member of the, beta-trefoil superfold, a protein architecture that exhibits a, characteristic threefold axis of structural symmetry. FGF-1 contains 11, beta-turns, the majority being type I 3:5; however, a type I 4:6 turn is, also found at three symmetry-related locations. The relative uniqueness of, the type I 4:6 turn in the FGF-1 structure suggests it may play a key role, in the stability, folding, or function of the protein. To test this, hypothesis a series of deletion mutations were constructed, the aim of, which was to convert existing type I 4:6 turns at two locations into type, I 3:5 turns. The results show it is possible to successfully substitute, the type I 4:6 turn by a type I 3:5 turn with minimal impact upon protein, stability or folding. Thus, these different turn structures, even though, they differ in length, exhibit similar energetic properties. Additional, sequence swapping mutations within the introduced type I 3:5 turns, suggests that the turn sequence primarily affects stability but not turn, structure (which appears dictated primarily by the local environment)., Although the results suggest that a stable, foldable beta-trefoil protein, may be designed utilizing a single turn type (type I 3:5), a type I 4:6, turn at turn 1 of FGF-1 appears essential for efficient mitogenic, function.
About this Structure
2AQZ is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Conversion of type I 4:6 to 3:5 beta-turn types in human acidic fibroblast growth factor: effects upon structure, stability, folding, and mitogenic function., Lee J, Dubey VK, Somasundaram T, Blaber M, Proteins. 2006 Mar 15;62(3):686-97. PMID:16355415
Page seeded by OCA on Wed Jan 23 15:23:25 2008
Categories: Homo sapiens | Single protein | Blaber, M. | Lee, J. | SO4 | Beta-trefoil
