1n73: Difference between revisions

New page: left|200px<br /><applet load="1n73" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n73, resolution 2.90Å" /> '''Fibrin D-Dimer, Lamp...
 
No edit summary
Line 1: Line 1:
[[Image:1n73.gif|left|200px]]<br /><applet load="1n73" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1n73.gif|left|200px]]<br /><applet load="1n73" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1n73, resolution 2.90&Aring;" />
caption="1n73, resolution 2.90&Aring;" />
'''Fibrin D-Dimer, Lamprey complexed with the PEPTIDE LIGAND: GLY-HIS-ARG-PRO-AMIDE'''<br />
'''Fibrin D-Dimer, Lamprey complexed with the PEPTIDE LIGAND: GLY-HIS-ARG-PRO-AMIDE'''<br />


==Overview==
==Overview==
The crystal structure of fragment double-D from factor XIII-cross-linked, lamprey fibrin has been determined at 2.9 A resolution. The 180 kDa, covalent dimer was cocrystallized with the peptide Gly-His-Arg-Pro-amide, which in many fibrinogens, but not that of lamprey, corresponds to the, B-knob exposed by thrombin. The structure was determined by molecular, replacement, a recently determined structure of lamprey fragment D being, used as a search model. GHRPam was found in both the gamma- and beta-chain, holes. Unlike the situation with fragment D, the crystal packing of the, cross-linked double-D structure exhibits two different D-D interfaces, each gamma-chain facing gamma-chains on two other molecules. One of these, (interface I) involves the asymmetric interface observed in all other D, fragments and related structures. The other (interface II) encompasses a, completely different set of residues. The two abutments differ in that, interface I results in an "in line" arrangement of abutting molecules and, the interface II in a "zigzag" arrangement. So far as can be determined, (the electron density could only be traced on one side of the, cross-links), it is the gamma-chains of the newly observed zigzag units, (interface II) that are joined by the reciprocal, epsilon-amino-gamma-glutamyl cross-links. Auspiciously, the same novel D-D, interface was observed in two lower-resolution crystal structures of human, double-D preparations that had been crystallized under unusual, circumstances. These observations show that double-D structures are linked, in a way that is sufficiently flexible to accommodate different D-D, interfaces under different circumstances.
The crystal structure of fragment double-D from factor XIII-cross-linked lamprey fibrin has been determined at 2.9 A resolution. The 180 kDa covalent dimer was cocrystallized with the peptide Gly-His-Arg-Pro-amide, which in many fibrinogens, but not that of lamprey, corresponds to the B-knob exposed by thrombin. The structure was determined by molecular replacement, a recently determined structure of lamprey fragment D being used as a search model. GHRPam was found in both the gamma- and beta-chain holes. Unlike the situation with fragment D, the crystal packing of the cross-linked double-D structure exhibits two different D-D interfaces, each gamma-chain facing gamma-chains on two other molecules. One of these (interface I) involves the asymmetric interface observed in all other D fragments and related structures. The other (interface II) encompasses a completely different set of residues. The two abutments differ in that interface I results in an "in line" arrangement of abutting molecules and the interface II in a "zigzag" arrangement. So far as can be determined (the electron density could only be traced on one side of the cross-links), it is the gamma-chains of the newly observed zigzag units (interface II) that are joined by the reciprocal epsilon-amino-gamma-glutamyl cross-links. Auspiciously, the same novel D-D interface was observed in two lower-resolution crystal structures of human double-D preparations that had been crystallized under unusual circumstances. These observations show that double-D structures are linked in a way that is sufficiently flexible to accommodate different D-D interfaces under different circumstances.


==About this Structure==
==About this Structure==
1N73 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 NAG and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N73 OCA].  
1N73 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=NAG:'>NAG</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N73 OCA].  


==Reference==
==Reference==
Line 13: Line 13:
[[Category: Petromyzon marinus]]
[[Category: Petromyzon marinus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Doolittle, R.F.]]
[[Category: Doolittle, R F.]]
[[Category: Pandi, L.]]
[[Category: Pandi, L.]]
[[Category: Yang, Z.]]
[[Category: Yang, Z.]]
Line 20: Line 20:
[[Category: isopeptide cross-linked chains; protein-peptide complex]]
[[Category: isopeptide cross-linked chains; protein-peptide complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:00:49 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:58 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA