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1bik

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X-RAY STRUCTURE OF BIKUNIN FROM THE HUMAN INTER-ALPHA-INHIBITOR COMPLEX

Structural highlights

1bik is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMBP_HUMAN Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization.^[1] Trypstatin is a trypsin inhibitor (By similarity).^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bikunin is a serine protease inhibitor found in the blood serum and urine of humans and other animals. Its sequence shows internal repetition, suggesting that it contains two domains that resemble bovine pancreatic trypsin inhibitor (BPTI). A fragment of bikunin has been crystallised, its structure solved and subsequently refined against 2.5 A data. The two BPTI-like domains pack closely together and are related by an approximate 60 degrees rotation combined with a translation. These domains are very similar to each other and other proteins with this fold. The largest variations occur in the loops responsible for protease recognition. The loops of the first domain are unobstructed by the remaining protein. However, the loops of the second domain are close to the first domain and it is possible that protease binding may be affected or, in some cases, abolished by the presence of the first domain. Thus, cleavage of the two domains could alter the substrate specificity of domain II. Bikunin has a hydrophobic patch close to the N terminus of domain I, which is the most likely site for cell-surface receptor binding. In addition, there is a basic patch at one end of domain II that may be responsible for the inhibition of calcium oxalate crystallization in urine.

The crystal structure of bikunin from the inter-alpha-inhibitor complex: a serine protease inhibitor with two Kunitz domains.,Xu Y, Carr PD, Guss JM, Ollis DL J Mol Biol. 1998 Mar 13;276(5):955-66. PMID:9566199^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Atmani F, Khan SR. Characterization of uronic-acid-rich inhibitor of calcium oxalate crystallization isolated from rat urine. Urol Res. 1995;23(2):95-101. PMID:7676539
↑ Atmani F, Khan SR. Characterization of uronic-acid-rich inhibitor of calcium oxalate crystallization isolated from rat urine. Urol Res. 1995;23(2):95-101. PMID:7676539
↑ Xu Y, Carr PD, Guss JM, Ollis DL. The crystal structure of bikunin from the inter-alpha-inhibitor complex: a serine protease inhibitor with two Kunitz domains. J Mol Biol. 1998 Mar 13;276(5):955-66. PMID:9566199 doi:10.1006/jmbi.1997.1582

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bik"

@@ Line 1: / Line 1: @@
 ==X-RAY STRUCTURE OF BIKUNIN FROM THE HUMAN INTER-ALPHA-INHIBITOR COMPLEX==
-<StructureSection load='1bik' size='340' side='right' caption='[[1bik]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='1bik' size='340' side='right'caption='[[1bik]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bik]] is a 1 chain structure with 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=1BIK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BIK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bik]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BIK FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bik OCA], [http://pdbe.org/1bik PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bik RCSB], [http://www.ebi.ac.uk/pdbsum/1bik PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1bik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bik OCA], [https://pdbe.org/1bik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bik RCSB], [https://www.ebi.ac.uk/pdbsum/1bik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bik ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AMBP_HUMAN AMBP_HUMAN]] Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization.<ref>PMID:7676539</ref>   Trypstatin is a trypsin inhibitor (By similarity).<ref>PMID:7676539</ref>
+[https://www.uniprot.org/uniprot/AMBP_HUMAN AMBP_HUMAN] Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization.<ref>PMID:7676539</ref>   Trypstatin is a trypsin inhibitor (By similarity).<ref>PMID:7676539</ref>
 == 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/bi/1bik_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bi/1bik_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1bik ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 32: / Line 34: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Carr, P D]]
+[[Category: Large Structures]]
-[[Category: Guss, J M]]
+[[Category: Carr PD]]
-[[Category: Ollis, D L]]
+[[Category: Guss JM]]
-[[Category: Xu, Y]]
+[[Category: Ollis DL]]
-[[Category: Bikunin]]
+[[Category: Xu Y]]
-[[Category: Glycoprotein]]
-[[Category: Glycosylated protein]]
-[[Category: Trypstatin]]
-[[Category: Urinary trypsin inhibitor]]
-[[Category: Uronic-acid-rich protein]]

1bik

From Proteopedia

Current revision

X-RAY STRUCTURE OF BIKUNIN FROM THE HUMAN INTER-ALPHA-INHIBITOR COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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