View source for 1ij9


==Highly Hydrated Human VCAM-1 Fragment==
<StructureSection load='1ij9' size='340' side='right'caption='[[1ij9]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ij9]] 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=1IJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IJ9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</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=1ij9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ij9 OCA], [https://pdbe.org/1ij9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ij9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ij9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ij9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VCAM1_HUMAN VCAM1_HUMAN] Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation.
== 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/ij/1ij9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ij9 ConSurf].
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== Publication Abstract from PubMed ==
An X-ray crystal structure of two N-terminal integrin-binding IgSF domains of human VCAM-1 is reported. This new crystal form shows an unusual and highly hydrated packing arrangement in which over 80% of the crystal is occupied by solvent. The relative orientations of the two domains adopt a new intermediate conformation. The tilt angle between the two domains is 19.4 degrees, compared with other related structures that have tilt angles ranging from 7.3 to 39.9 degrees. An analysis of the torsion angles shows that residues Ile88, Tyr89, Ser90, Pro92 and Glu96 play a major role in defining the interdomain conformations.

A new conformation of the integrin-binding fragment of human VCAM-1 crystallizes in a highly hydrated packing arrangement.,Taylor P, Bilsland M, Walkinshaw MD Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1579-83. Epub 2001, Oct 25. PMID:11679722<ref>PMID:11679722</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bilsland M]]
[[Category: Taylor P]]
[[Category: Walkinshaw MD]]