1n73: Difference between revisions

Revision as of 10:27, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n73.png

Template:STRUCTURE 1n73

Fibrin D-Dimer, Lamprey complexed with the PEPTIDE LIGAND: GLY-HIS-ARG-PRO-AMIDEFibrin D-Dimer, Lamprey complexed with the PEPTIDE LIGAND: GLY-HIS-ARG-PRO-AMIDE

Template:ABSTRACT PUBMED 12501189

About this StructureAbout this Structure

1N73 is a Protein complex structure of sequences from Petromyzon marinus. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of fragment double-D from cross-linked lamprey fibrin reveals isopeptide linkages across an unexpected D-D interface., Yang Z, Pandi L, Doolittle RF, Biochemistry. 2002 Dec 31;41(52):15610-7. PMID:12501189

Page seeded by OCA on Mon Jul 28 10:27:10 2008

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OCA

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-[[Image:1n73.gif|left|200px]]
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 {{STRUCTURE_1n73|  PDB=1n73  |  SCENE=  }}
-'''Fibrin D-Dimer, Lamprey complexed with the PEPTIDE LIGAND: GLY-HIS-ARG-PRO-AMIDE'''
+===Fibrin D-Dimer, Lamprey complexed with the PEPTIDE LIGAND: GLY-HIS-ARG-PRO-AMIDE===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_12501189}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12501189 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12501189}}
 ==About this Structure==
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 [[Category: Isopeptide cross-linked chain]]
 [[Category: Protein-peptide complex]]
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