This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1kdu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1kdu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kdu" /> '''SEQUENTIAL 1H NMR ASSIGNMENTS AND SECONDARY...)
Current revision (07:59, 3 April 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1kdu.gif|left|200px]]<br />
 
-
<applet load="1kdu" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1kdu" />
 
-
'''SEQUENTIAL 1H NMR ASSIGNMENTS AND SECONDARY STRUCTURE OF THE KRINGLE DOMAIN FROM UROKINASE'''<br />
 
-
==Overview==
+
==SEQUENTIAL 1H NMR ASSIGNMENTS AND SECONDARY STRUCTURE OF THE KRINGLE DOMAIN FROM UROKINASE==
-
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.
+
<StructureSection load='1kdu' size='340' side='right'caption='[[1kdu]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1kdu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KDU FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdu OCA], [https://pdbe.org/1kdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kdu RCSB], [https://www.ebi.ac.uk/pdbsum/1kdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kdu ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[https://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN] Defects in PLAU are the cause of Quebec platelet disorder (QPD) [MIM:[https://omim.org/entry/601709 601709]. QPD is an autosomal dominant bleeding disorder due to a gain-of-function defect in fibrinolysis. Although affected individuals do not exhibit systemic fibrinolysis, they show delayed onset bleeding after challenge, such as surgery. The hallmark of the disorder is markedly increased PLAU levels within platelets, which causes intraplatelet plasmin generation and secondary degradation of alpha-granule proteins.<ref>PMID:20007542</ref>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN] Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kd/1kdu_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kdu ConSurf].
 +
<div style="clear:both"></div>
-
==Disease==
+
==See Also==
-
Known disease associated with this structure: Alzheimer disease, late-onset, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191840 191840]]
+
*[[Plasminogen activator|Plasminogen activator]]
-
 
+
*[[Urokinase 3D Structures|Urokinase 3D Structures]]
-
==About this Structure==
+
== References ==
-
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].
+
<references/>
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1327118 1327118]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Bokman, A.M.]]
+
[[Category: Bokman AM]]
-
[[Category: Dobson, C.M.]]
+
[[Category: Dobson CM]]
-
[[Category: Li, X.]]
+
[[Category: Li X]]
-
[[Category: Llinas, M.]]
+
[[Category: Llinas M]]
-
[[Category: Smith, R.A.G.]]
+
[[Category: Smith RAG]]
-
[[Category: plasminogen activation]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:50:11 2007''
+

Current revision

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

PDB ID 1kdu

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kdu"
Personal tools