1kdu: Difference between revisions

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New page: left|200px<br /> <applet load="1kdu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kdu" /> '''SEQUENTIAL 1H NMR ASSIGNMENTS AND SECONDARY...
 
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[[Image:1kdu.gif|left|200px]]<br />
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<applet load="1kdu" size="450" color="white" frame="true" align="right" spinBox="true"  
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'''SEQUENTIAL 1H NMR ASSIGNMENTS AND SECONDARY STRUCTURE OF THE KRINGLE DOMAIN FROM UROKINASE'''<br />
'''SEQUENTIAL 1H NMR ASSIGNMENTS AND SECONDARY STRUCTURE OF THE KRINGLE DOMAIN FROM UROKINASE'''<br />
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==About this Structure==
==About this Structure==
1KDU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KDU OCA].  
1KDU is a [http://en.wikipedia.org/wiki/Single_protein 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=1KDU OCA].  


==Reference==
==Reference==
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[[Category: plasminogen activation]]
[[Category: plasminogen activation]]


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Revision as of 17:12, 15 February 2008

File:1kdu.jpg


1kdu

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SEQUENTIAL 1H NMR ASSIGNMENTS AND SECONDARY STRUCTURE OF THE KRINGLE DOMAIN FROM UROKINASE

OverviewOverview

The sequence-specific 1H NMR assignments of the 89-residue recombinant, kringle domain from human urokinase are presented. These were achieved, primarily by utilizing TOCSY and NOESY spectra in conjunction with COSY, spectra recorded at 500 MHz and 600 MHz. Regular secondary structure, elements have been derived from a qualitative interpretation of nuclear, Overhauser enhancement, JNH alpha coupling constant, and amide proton, exchange data. Two helices have been identified. One helix, involving, Ser40-Gly46, corresponds to that reported for t-PA kringle 2 (Byeon et, al., 1991), but does not exist in other kringles with known structures., The second helix, in the region Asn26-Gln33, is thus far unique to the, urokinase kringle. Three antiparallel beta-sheets and three tight turns, have also been identified, which correspond exactly to those identified in, t-PA kringle 2 both in solution and in the crystalline state (de Vos et, al., 1992). Despite the very different ligand binding properties of the, urokinase kringle, NOE data indicate that the tertiary fold of the, molecule conforms closely to that found for other kringles.

DiseaseDisease

Known disease associated with this structure: Alzheimer disease, late-onset, susceptibility to OMIM:[191840]

About this StructureAbout this Structure

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

ReferenceReference

Sequential 1H NMR assignments and secondary structure of the kringle domain from urokinase., Li X, Smith RA, Dobson CM, Biochemistry. 1992 Oct 13;31(40):9562-71. PMID:1327118

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