2ci2

<table><tr><td colspan='2'>[[2ci2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Barley Barley]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ci2 1ci2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CI2 FirstGlance]. <br>

</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=2ci2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ci2 OCA], [https://pdbe.org/2ci2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ci2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ci2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ci2 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/ICI2_HORVU ICI2_HORVU]] Inhibits both subtilisin and chymotrypsin.

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== Publication Abstract from PubMed ==

Chymotrypsin inhibitor 2 (CI-2), a serine proteinase inhibitor from barley seeds, has been crystallized and its three-dimensional structure determined at 2.0-A resolution by the molecular replacement method. The structure has been refined by restrained-parameter least-squares methods to a crystallographic R factor (= sigma parallel Fo magnitude of-Fo parallel/sigma magnitude of Fo) o of 0.198. CI-2 is a member of the potato inhibitor 1 family. It lacks the characteristic stabilizing disulfide bonds of most other members of serine proteinase inhibitor families. The body of CI-2 shows few conformational changes between the free inhibitor and the previously reported structure of CI-2 in complex with subtilisin Novo [McPhalen, C.A., Svendsen, I., Jonassen, I., &amp; James, M.N.G. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7242-7246]. However, the reactive site loop has some significant conformational differences between the free inhibitor and its complexed form. The residues in this segment of polypeptide exhibit relatively large thermal motion parameters and some disorder in the uncomplexed form of the inhibitor. The reactive site bond is between Met-59I and Glu-60I in the consecutive sequential numbering of CI-2 (Met-60-Glu-61 according to the alignment of Svendsen et al. [Svendsen, I., Hejgaard, J., &amp; Chavan, J.K. (1984) Carlsberg Res. Commun. 49, 493-502]). The network of hydrogen bonds and electrostatic interactions stabilizing the conformation of the reactive site loop is much less extensive in the free than in the complexed inhibitor.

Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds.,McPhalen CA, James MN Biochemistry. 1987 Jan 13;26(1):261-9. PMID:3828302<ref>PMID:3828302</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2ci2" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Barley]]

[[Category: James, M N.G]]

[[Category: Mcphalen, C A]]