1krn

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[[Image:1krn.jpg|left|200px]]<br /><applet load="1krn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1krn.jpg|left|200px]]
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caption="1krn, resolution 1.67&Aring;" />
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'''STRUCTURE OF KRINGLE 4 AT 4C TEMPERATURE AND 1.67 ANGSTROMS RESOLUTION'''<br />
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{{Structure
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|PDB= 1krn |SIZE=350|CAPTION= <scene name='initialview01'>1krn</scene>, resolution 1.67&Aring;
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|SITE= <scene name='pdbsite=SO4:Sulfate+Binding+Site.+The+Active+Site+Also+Contains+Resi+...'>SO4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Plasmin Plasmin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.7 3.4.21.7]
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|GENE=
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}}
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'''STRUCTURE OF KRINGLE 4 AT 4C TEMPERATURE AND 1.67 ANGSTROMS RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1KRN 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]. Active as [http://en.wikipedia.org/wiki/Plasmin Plasmin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.7 3.4.21.7] Known structural/functional Site: <scene name='pdbsite=SO4:Sulfate+Binding+Site.+The+Active+Site+Also+Contains+Resi+...'>SO4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRN OCA].
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1KRN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRN OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299951 15299951]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15299951 15299951]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Plasmin]]
[[Category: Plasmin]]
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[[Category: serine protease]]
[[Category: serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:21:16 2008''

Revision as of 10:21, 20 March 2008

Image:1krn.jpg


PDB ID 1krn

Drag the structure with the mouse to rotate
, resolution 1.67Å
Sites:
Ligands:
Activity: Plasmin, with EC number 3.4.21.7
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF KRINGLE 4 AT 4C TEMPERATURE AND 1.67 ANGSTROMS RESOLUTION


Contents

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.

Disease

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 Structure

1KRN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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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