1lwu
From Proteopedia
(New page: 200px<br /><applet load="1lwu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lwu, resolution 2.80Å" /> '''Crystal structure of...) |
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| - | [[Image:1lwu.gif|left|200px]]<br /><applet load="1lwu" size=" | + | [[Image:1lwu.gif|left|200px]]<br /><applet load="1lwu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lwu, resolution 2.80Å" /> | caption="1lwu, resolution 2.80Å" /> | ||
'''Crystal structure of fragment D from lamprey fibrinogen complexed with the peptide Gly-His-Arg-Pro-amide'''<br /> | '''Crystal structure of fragment D from lamprey fibrinogen complexed with the peptide Gly-His-Arg-Pro-amide'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of fragment D from lamprey fibrinogen has been | + | The crystal structure of fragment D from lamprey fibrinogen has been determined at 2.8 A resolution. The 89 kDa protein was cocrystallized with the peptide Gly-His-Arg-Pro-amide, which in many fibrinogens-but not lamprey-corresponds to the B knob exposed by thrombin. Because lamprey fragment D is more than 50% identical in sequence with human fragment D, the structure of which has been reported previously, it was possible to use the method of molecular replacement. The space group of the lamprey crystals is P1; there are four molecules in the unit cell. Although the fragments are packed head to head by the same D:D interface as is observed in other related preparations containing fragments D, the tails are uniquely joined by an unnatural association of the terminal sections of the residual coiled coils from adjacent molecules. Some features of the lamprey structure are clearer than have been observed in previous fragment D structures, including the beta-chain carbohydrate cluster, for one, and the important gamma-chain carboxyl-terminal segment, for another. The most significant differences between the lamprey and human structures occur in connecting loops at the entryways to the beta-chain and gamma-chain binding pockets. |
==About this Structure== | ==About this Structure== | ||
| - | 1LWU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Petromyzon_marinus Petromyzon marinus] with NDG, MAN, NAG, GAL, CA and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LWU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Petromyzon_marinus Petromyzon marinus] with <scene name='pdbligand=NDG:'>NDG</scene>, <scene name='pdbligand=MAN:'>MAN</scene>, <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=GAL:'>GAL</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LWU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Petromyzon marinus]] | [[Category: Petromyzon marinus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Doolittle, R | + | [[Category: Doolittle, R F.]] |
| - | [[Category: Everse, S | + | [[Category: Everse, S J.]] |
[[Category: Pandi, L.]] | [[Category: Pandi, L.]] | ||
[[Category: Riley, M.]] | [[Category: Riley, M.]] | ||
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[[Category: protein-peptide complex]] | [[Category: protein-peptide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:13 2008'' |
Revision as of 11:49, 21 February 2008
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Crystal structure of fragment D from lamprey fibrinogen complexed with the peptide Gly-His-Arg-Pro-amide
Overview
The crystal structure of fragment D from lamprey fibrinogen has been determined at 2.8 A resolution. The 89 kDa protein was cocrystallized with the peptide Gly-His-Arg-Pro-amide, which in many fibrinogens-but not lamprey-corresponds to the B knob exposed by thrombin. Because lamprey fragment D is more than 50% identical in sequence with human fragment D, the structure of which has been reported previously, it was possible to use the method of molecular replacement. The space group of the lamprey crystals is P1; there are four molecules in the unit cell. Although the fragments are packed head to head by the same D:D interface as is observed in other related preparations containing fragments D, the tails are uniquely joined by an unnatural association of the terminal sections of the residual coiled coils from adjacent molecules. Some features of the lamprey structure are clearer than have been observed in previous fragment D structures, including the beta-chain carbohydrate cluster, for one, and the important gamma-chain carboxyl-terminal segment, for another. The most significant differences between the lamprey and human structures occur in connecting loops at the entryways to the beta-chain and gamma-chain binding pockets.
About this Structure
1LWU is a Protein complex structure of sequences from Petromyzon marinus with , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of fragment D from lamprey fibrinogen complexed with the peptide Gly-His-Arg-Pro-amide., Yang Z, Spraggon G, Pandi L, Everse SJ, Riley M, Doolittle RF, Biochemistry. 2002 Aug 13;41(32):10218-24. PMID:12162736
Page seeded by OCA on Thu Feb 21 13:49:13 2008
Categories: Petromyzon marinus | Protein complex | Doolittle, R F. | Everse, S J. | Pandi, L. | Riley, M. | Spraggon, G. | Yang, Z. | CA | GAL | MAN | NAG | NDG | NH2 | Coiled coil | Heterotrimer | Protein-peptide complex
