1krn: Difference between revisions
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==Overview== | ==Overview== | ||
Despite considerable effort to elucidate the functional role of the, kringle domains, relatively little is known about interactions with other, protein domains. Most of the crystal structures describe the interactions, at the kringle active site. This study suggests a novel way to interpret, structural results such as disorder located away from an active site. The, crystal structure of human plasminogen kringle 4 (PGK4) has been refined, against 10-1.68 A resolution X-ray data (R(merge) = 3.7%) to the standard, crystallographic R = 14.7% using the program X-PLOR. The crystals of PGK4, showed significant instability in cell dimensions (changes more than 1.5, A) even at 277 K. The refinement revealed structural details not observed, before [Mulichak, Tulinsky & Ravichandran (1991). Biochemistry, 30, 10576-10588], such as clear density for additional side chains and more, extensive disorder. Discrete disorder was detected for residues S73, S78, T80, S89, S91, S92, Ml12, S132, C138 and K142. Most of the disordered, residues form two patches on the surface of the protein. This localized, disorder suggests that these residues may play a role in quaternary, interactions and possibly form an interface with the other domains of, proteins that contain kringles, such as plasminogen. Although, an, additional residue D65 was refined at the beginning of the sequence, still, more residues near the peptide cleavage site must be disordered in the, crystal. | Despite considerable effort to elucidate the functional role of the, kringle domains, relatively little is known about interactions with other, protein domains. Most of the crystal structures describe the interactions, at the kringle active site. This study suggests a novel way to interpret, structural results such as disorder located away from an active site. The, crystal structure of human plasminogen kringle 4 (PGK4) has been refined, against 10-1.68 A resolution X-ray data (R(merge) = 3.7%) to the standard, crystallographic R = 14.7% using the program X-PLOR. The crystals of PGK4, showed significant instability in cell dimensions (changes more than 1.5, A) even at 277 K. The refinement revealed structural details not observed, before [Mulichak, Tulinsky & Ravichandran (1991). Biochemistry, 30, 10576-10588], such as clear density for additional side chains and more, extensive disorder. Discrete disorder was detected for residues S73, S78, T80, S89, S91, S92, Ml12, S132, C138 and K142. Most of the disordered, residues form two patches on the surface of the protein. This localized, disorder suggests that these residues may play a role in quaternary, interactions and possibly form an interface with the other domains of, proteins that contain kringles, such as plasminogen. Although, an, additional residue D65 was refined at the beginning of the sequence, still, more residues near the peptide cleavage site must be disordered in the, crystal. | ||
==Disease== | |||
Known diseases associated with this structure: Conjunctivitis, ligneous OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173350 173350]], Plasminogen Tochigi disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173350 173350]], Plasminogen deficiency, types I and II OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173350 173350]], Thrombophilia, dysplasminogenemic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173350 173350]] | |||
==About this Structure== | ==About this Structure== | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:53:55 2007'' | ||
Revision as of 18:47, 12 November 2007
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STRUCTURE OF KRINGLE 4 AT 4C TEMPERATURE AND 1.67 ANGSTROMS RESOLUTION
OverviewOverview
Despite considerable effort to elucidate the functional role of the, kringle domains, relatively little is known about interactions with other, protein domains. Most of the crystal structures describe the interactions, at the kringle active site. This study suggests a novel way to interpret, structural results such as disorder located away from an active site. The, crystal structure of human plasminogen kringle 4 (PGK4) has been refined, against 10-1.68 A resolution X-ray data (R(merge) = 3.7%) to the standard, crystallographic R = 14.7% using the program X-PLOR. The crystals of PGK4, showed significant instability in cell dimensions (changes more than 1.5, A) even at 277 K. The refinement revealed structural details not observed, before [Mulichak, Tulinsky & Ravichandran (1991). Biochemistry, 30, 10576-10588], such as clear density for additional side chains and more, extensive disorder. Discrete disorder was detected for residues S73, S78, T80, S89, S91, S92, Ml12, S132, C138 and K142. Most of the disordered, residues form two patches on the surface of the protein. This localized, disorder suggests that these residues may play a role in quaternary, interactions and possibly form an interface with the other domains of, proteins that contain kringles, such as plasminogen. Although, an, additional residue D65 was refined at the beginning of the sequence, still, more residues near the peptide cleavage site must be disordered in the, crystal.
DiseaseDisease
Known diseases associated with this structure: Conjunctivitis, ligneous OMIM:[173350], Plasminogen Tochigi disease OMIM:[173350], Plasminogen deficiency, types I and II OMIM:[173350], Thrombophilia, dysplasminogenemic OMIM:[173350]
About this StructureAbout this Structure
1KRN is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Active as Plasmin, with EC number 3.4.21.7 Structure known Active Site: SO4. Full crystallographic information is available from OCA.
ReferenceReference
Structure of human plasminogen kringle 4 at 1.68 a and 277 K. A possible structural role of disordered residues., Stec B, Yamano A, Whitlow M, Teeter MM, Acta Crystallogr D Biol Crystallogr. 1997 Mar 1;53(Pt 2):169-78. PMID:15299951
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