1k5v

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(New page: 200px<br /> <applet load="1k5v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k5v, resolution 2.10&Aring;" /> '''Human acidic fibrob...)
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<applet load="1k5v" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1k5v, resolution 2.10&Aring;" />
'''Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with Asn106 replaced by Gly (N106G).'''<br />
'''Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with Asn106 replaced by Gly (N106G).'''<br />
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==About this Structure==
==About this Structure==
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1K5V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K5V OCA].
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1K5V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K5V OCA].
==Reference==
==Reference==
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[[Category: beta-trefoil]]
[[Category: beta-trefoil]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:47:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:11:41 2008''

Revision as of 14:11, 15 February 2008


1k5v, resolution 2.10Å

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Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with Asn106 replaced by Gly (N106G).

Contents

Overview

Human acidic fibroblast growth factor (FGF-1) has a beta-trefoil, structure, one of the fundamental protein superfolds. The X-ray crystal, structures of wild-type and various mutant forms of FGF-1 have been solved, in five different space groups: C2, C222(1), P2(1) (four molecules/asu), P2(1) (three molecules/asu), and P2(1)2(1)2(1). These structures reveal, two characteristically different conformations for the beta8/beta9, beta-hairpin comprising residue positions 90-94. This region in the, wild-type FGF-1 structure (P2(1), four molecules/asu), a his-tagged, His93-->Gly mutant (P2(1), three molecules/asu) and a his-tagged, Asn106-->Gly mutant (P2(1)2(1)2(1)) adopts a 3:5 beta-hairpin known as a, type I (1-4) G1 beta-bulge (containing a type I turn). However, a, his-tagged form of wild-type FGF-1 (C222(1)) and a his-tagged Leu44-->Phe, mutant (C2) adopt a 3:3 beta-hairpin (containing a type I' turn) for this, same region. A feature that distinguishes these two types of beta-hairpin, structures is the number and location of side chain positions with, eclipsed C(beta) and main-chain carbonyl oxygen groups (Psi is equivalent, to +60 degrees). The effects of glycine mutations upon stability, at, positions within the hairpin, have been used to identify the most likely, structure in solution. Type I' turns in the structural data bank are quite, rare, and a survey of these turns reveals that a large percentage exhibit, crystal contacts within 3.0 A. This suggests that many of the type I', turns in X-ray structures may be adopted due to crystal packing effects.

Disease

Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[602115], LADD syndrome OMIM:[602115]

About this Structure

1K5V is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Alternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factor., Kim J, Blaber SI, Blaber M, Protein Sci. 2002 Mar;11(3):459-66. PMID:11847269

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