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1krn

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[[Category: serine protease]]
[[Category: serine protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:52:56 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:41:37 2007''

Revision as of 13:36, 30 October 2007

Image:1krn.gif

1krn, resolution 1.67Å

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

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). ... [(full description)]

About 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].

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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